Computational prediction of the tertiary structure of the human iduronate 2-sulfate sulfatase
Keywords:
mucopolysaccharidosis II, iduronate sulfatase, tertiary protein structure, computing methods
Abstract
Introduction. Hunter syndrome (MC KUSIK 309900) or mucopolysacharidosis type II is due to the deficiency of the enzyme iduronate 2 sulfate sulfatase (E.C. 3.1.6.13). This enzyme has not been crystallized, and therefore the experimental structures are not available. Objectives. A computational three-dimensional model was proposed for the iduronate 2 sulfate sulfatase enzyme.Materials and methods. A computational analysis of this enzyme used the following free internet software programs: Comput pI/MW, JaMBW Chapter 3.1.7, SWISS-MODEL, Geno3d, ProSup. Energy minimization was done with Discover 3 and Insight II version 2004.
Results. A three-dimensional conformational model was proposed. The model showed 33.3% of helix structure, 7.2% beta sheet, and 59.5% random coil. RMS values (Root Mean Square) (0.78 and 0.86Å) were found when compared with other enzymes of the same family. The model presented 5 exposed N-glycosylation potential sites and an entry to the pocket that contains the amino acids of the active site. A high correlation was found between the type of mutations and the severity of the phenotype in twenty patients analyzed.
Conclusion. The RMS values, as well as the high correlation between the type of mutation and the phenotype, indicated that the model predicts some aspects of the enzyme's biological behavior.
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References
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3. Young ID, Harper PS. Incidence of Hunter's syndrome. Hum Genet 1982;60:391-2.
4. Lowry R, Applegarth D, Toone J, Macdonald E, Thunem N. An update on the frequency of mucopolysaccharide syndromes in British Columbia. Hum Genet 1990;85:389-90.
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10. Bunge S, Rathmann M, Steglich C, Bondeson ML, Tylki-Szymanska A, Popowska E et al. Homologous nonallelic between the iduronate-sulfatase gene and pseudogene cause various intragenic deletions and
inversions in patients with mucopolysaccharidosis type II. Eur J Hum Genet 1998;6:492-500.
11. Froissart R, Maire I, Millat G, Cudry S, Birot AM, Bonnet V et al. Identification of iduronate sulfatase gene alterations in 70 unrelated Hunter patients. Clin Genet 1998;53:362-8.
12. Gort L, Chabas A, Coll MJ. Hunter disease in the Spanish population: molecular analysis in 31 families. J Inherit Metab Dis 1998;21:655-61.
13. Isogai K, Sukegawa K, Tomatsu S, Fukao T, Song XQ, Yamada Y et al. Mutation analysis in the iduronate-2-sulphatase gene in 43 Japanese patients with mucopolysaccharidosis type II (Hunter disease). J Inherit Metab Dis 1998;21:60-70.
14. Karsten S, Voskoboeva E, Tishkanina S, Pettersson U, Krasnopolskaja X, Bondenson M. Mutational spectrum if the iduronate-2-sulfatase (IDS) gene in 36 unrelated Russian MPS II patients. Hum Genet
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15. Vafiadaki E, Cooper A, Heptinstall LE, Hatton CE, Thornley M, Wraith JE. Mutation analysis in 57 unrelated patients with MPS II (Hunter's disease). Arch Dis Child 1998;79:237-41.
16. Li P, Bellows AB, Thompson JN. Molecular basis of iduronate 2-sulfatase gene mutations in patients with mucopolysaccharidosis type II (Hunter syndrome). J Med Genet 1999;36:21-7.
17. Vallance HO, Bernard L, Rashed M, Chiu D, Le G, Toone J et al. Identification of 6 novel mutation in the iduronate sulfatase gene. Mutation in brief 233. Online. Hum Mutat 1999;13:338.
18. Cudry S, Tigaud I, Froissart R, Bonnet V, Maire I, Bozon D. MPS II in females: Molecular basis of two different cases. J Med Genet 2000;37:E29.
19. Bonuccelli G, Di Natale P, Corsolini F, Villani G, Regis S, Filocamo M. The effect of four mutations on the expression of iduronate-2-sulfatase in mucopolysaccharidosis type II. Biochem Biophys Acta 2001;1537:233-8.
20. Filocamo M, Bonuccelli G, Corsolini F, Mazzotti R, Cusano R, Gatti R. Molecular analysis of 40 Italian patients with mucopolysaccharidosis type II: New mutation in the iduronate-2-sulfatase (IDS) gene. Hum Mutat 2001;21:164-5.
21. Moreira da Silva I, Froissart R, Marques dos Santos H, Caseiro C, Maire I, Bozon D. Molecular basis of mucopolysaccharidosis type II in Portugal: Identification of four novel mutations. Clin Genet 2001;60:316-8.
22. Ricci V, Regis S, Di Duca M, Filocamo M. An Alumediated rearrangement as cause of exon skipping in Hunter disease. Hum Genet 2003;112:419-25.
23. Kim CH, Hwang HZ, Song SM, Paik KH, Kwon EK, Moon KB et al. Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: Identification of 13 novel mutations. Hum Mutat 2003;21:449-50.
24. Tomatsu S, Orii KO, Bi Y, Gutierrez MA, Nishioka T, Yamaguchi S et al. General implications for CpG hot spot mutations: methylation patterns of the human iduronate-2-sulfatase gene locus. Hum Mutat 2004;23:590-8.
25. Parkinson EJ, Muller V, Hopwood JJ, Brooks DA. Iduronate 2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients. Mol Genet Metab 2004;81:58-64.
26. Chang JH, Lin SP, Lin SC, Tseng KL, Li CL, Chuang CK et al. Expression studies of mutations underlying Taiwanese Hunter syndrome (mucopolysaccharidosis type II). Hum Genet 2005;116:160-6.
27. Tomatsu S, Sukegawa K, Trandafirescu GG, Gutierrez MA, Nishioka T, Yamaguchi S et al. Differences in methylation patterns in the methylation boundary region of IDS gene in Hunter syndrome patients: implications for CpG hot spot mutations. Eur J Hum Genet 2006;14:838-45.
28. Wilson PJ, Morris CP, Anson DS, Occhiodoro T, Bielick J, Clements PR et al. Hunter syndrome: Isolation of an Iduronate 2-sulfatase cDNA clone and analysis of patients DNA. Proc Natl Acad Sci USA
1990;87:8531-5.
29. Wilson PJ, Meaney CA, Hopwood JJ, Morris CP. Sequence of the human iduronate 2-sulfatase (IDS) gene. Genomics 1993;17:773-5.
30. Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins M, Appel R et al. Protein identification and analysis tools on the expasy server. En: Walker JM, editor. The proteomics protocols handbook. New York, USA: Human Press; 2005. p.571-660.
31. Bjellqvist B, Hughes GJ, Pasquali C, Paquet N, Ravier F, Sánchez JC et al. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 1993;14:1023-31.
32. Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999;294:1351-62.
33. Julenius K, Molgaard G, Gupta R, Brunak S. Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 2005;15:153-64.
34. Blon N, Ponten T, Gupta R, Brunak S. Prediction of post-translational glycosilation and phosphorylation of proteins from aminoacid sequence. Proteomics 2004;4:1633-49.
35. Frith MC, Spoge JL, Hansen U, Weng Z. Statistical significance of clusters of motifs represented by position specific scoring matrices in nucleotide sequences. Nucleic Acids Res 2002;30:3214-24.
36. Hopp TP, Woods KR. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 1981;78:3824-8.
37. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W et al. Gapped Blast and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 1997;25:3389-402.
38. Kneller DG, Cohen FE, Langridge R. Improvements in protein secondary structure prediction by an enhanced neural network. J Mol Biol 1990;214:171-82.
39. Garnier J, Gibrat J, Robson B, Doolittle R. Gor secondary structure prediction method version iv. Methods Enzymol 1996;266:540-53.
40. Guex N, Peitisch M. SWISS-MODEL and the Swiss- PdbViewer: An environment for comparative protein modeling. Electrophoresis 1997;18:2714-23.
41. Cuff JA, Clamp ME, Siddiqui AS, Finlay M, Barton GJ. JPred: A consensus secondary structure prediction server. Bioinformatics 1998;14:892-3.
42. Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292:195-202.
43. Shindyalov IN, Bourne PE. A database and tools for 3-D protein structure comparison and alignment using the Combinatorial Extension (CE) algorithm. Nucleic Acids Res 2001:29:228-9.
44. Pollastri G, Przybylski D, Rost B, Baldi P. Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 2002;47:228-35.
45. Muñoz V, Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J Mol Biol 1994;245:275-96.
46. Combet C, Jambon M, Deléage G, Geourjon C. Geno3d: Automatic comparative molecular modeling of protein. Bioinformatics 2002;18:213-4.
47. Lambert C, Leonard N, De Bolle X, Depiereux E. ESyPred3d: Prediction of proteins 3D structures. Bioinformatics 2002;18:1250-6.
48. Discover©. Accelrys software Inc. San Diego, USA: Accelrys software Inc; 2001-2006.
49. Sayle RA, Milner-White EJ. RASMOL: Biomolecular graphics for all. Trends Biochem Sci 1995;20:374.
50. Schmidt B, Selmer T, Ingendoh A, von Figura K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency cell. Cell 1995;82:271-8.
51. Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ et al. Structure of human lysosomal sulfatase. Structure 1997;5:277-89.
52. Parenti G, Meroni G, Ballabio A. The sulfatase gene family. Curr Opin Genet Dev 1997;7:386-91.
53. Dierks T, Lecca M, Schlotterhose P, Schmidt B, von Figura K. Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases. EMBO J 1999;18:2084-91.
54. Waldow A, Schmidt B, Dierks T, Von Bulow R, von Figura K. Amino acid residues forming the active site of arylsulfatase A. Role in catalytic activity and substrate binding. J Biol Chem 1999;274:12284-8.
55. Web Lab Viewer Pro. Web Lab, Molecular Simulation. Getting Starting. Ca, USA: Web Lab Viewer Pro; 2000.
56. Baker D, Sali A. Protein structure prediction and structural genomics. Science 2001;294:93-6.
57. Chothia C, Lesk AM. The relation between the divergence of sequence and structure in proteins. EMBO J 1986;5:823-6.
58. Stemberg M. Protein structure prediction. Oxford: IRL Press; 1996. p.298.
59. Froissart R, Millat G, Mathiu M, Bozon D, Maire I. Processing of iduronate 2-sulfatase in human fibroblasts. Biochem J 1995;309:425-30.
60. Millat G, Froissart R, Maire I, Bozon D. Characterization of iduronate sulfate sulfatase mutants affecting N-glycosylations sites and cysteine-84 residue. Biochem J 1997;326:243-7.
61. Millat G, Froissart R, Maire I, Bozon D. IDS transfer from overexpressing cell to IDS-deficient. Exp Cell Res 1997;230:362-7.
62. Sosa A, Barrera L. Production of specific chicken egg yolk antibodies to Iduronate 2-sulphate sulphatase (IDS) and its applicability in an Enzime-Linked Immunosorbent Assay (Elisa). J Inherit Metab Dis 2005;28(Suppl.1);185.
63. Sáenz H. Expresión, purificación parcial y estudios computacionales de la IDShr producida en Pichia pastoris. (Tesis Doctoral). Bogotá D.C.: Facultad de Ciencias, Pontificia Universidad Javeriana; 2005. p.149.
2. Schaap T, Bach G. Incidence of mucopolysaccharidoses in Israel: is Hunter disease a "Jewish disease"? Hum Genet 1980;56:221-3.
3. Young ID, Harper PS. Incidence of Hunter's syndrome. Hum Genet 1982;60:391-2.
4. Lowry R, Applegarth D, Toone J, Macdonald E, Thunem N. An update on the frequency of mucopolysaccharide syndromes in British Columbia. Hum Genet 1990;85:389-90.
5. Bunge S, Steligch C, Zuther C, Beck M, Morris CP, Schwinger E et al. Iduronate 2-sulfatase gene mutations in 16 patients with mucopolysaccharidosis type II. Hum Mol Genet 1993;2:1871-5.
6. Hopwood JJ, Bunge S, Morris CP, Wilson PJ, Steglich C, Beck M et al. Molecular basis of mucopolysaccharidosis type II: mutations in the iduronate-2-sulphatase gene. Hum Mutat 1993;2:435-42.
7. Jonsson JJ, Aronovich EL, Braun SE, Whitley CB. Molecular diagnosis of mucopolysaccharidosis type II (Hunter syndrome) by automated sequencing and computer- assisted interpretation: toward mutation mapping of the iduronate-2-sulfatase gene. Am J Hum Genet 1995;56:597-607.
8. Rathmann M, Bunge S, Beck M, Kresse H, Tylki-Szymanska A, Gal A. Mucopolysaccharidosis type II (Hunter syndrome): mutation "hot spots" in the iduronate-2-sulfatase gene. Am J Hum Genet 1996;59:1202-9.
9. Villani GR, Balzano N, Grosso M, Salvatore F, Izzo P, Di Natalie P. Mucopolysaccharidosis type II: Identification of six novel mutations in Italian patients. Hum Mutat 1997;10:71-5.
10. Bunge S, Rathmann M, Steglich C, Bondeson ML, Tylki-Szymanska A, Popowska E et al. Homologous nonallelic between the iduronate-sulfatase gene and pseudogene cause various intragenic deletions and
inversions in patients with mucopolysaccharidosis type II. Eur J Hum Genet 1998;6:492-500.
11. Froissart R, Maire I, Millat G, Cudry S, Birot AM, Bonnet V et al. Identification of iduronate sulfatase gene alterations in 70 unrelated Hunter patients. Clin Genet 1998;53:362-8.
12. Gort L, Chabas A, Coll MJ. Hunter disease in the Spanish population: molecular analysis in 31 families. J Inherit Metab Dis 1998;21:655-61.
13. Isogai K, Sukegawa K, Tomatsu S, Fukao T, Song XQ, Yamada Y et al. Mutation analysis in the iduronate-2-sulphatase gene in 43 Japanese patients with mucopolysaccharidosis type II (Hunter disease). J Inherit Metab Dis 1998;21:60-70.
14. Karsten S, Voskoboeva E, Tishkanina S, Pettersson U, Krasnopolskaja X, Bondenson M. Mutational spectrum if the iduronate-2-sulfatase (IDS) gene in 36 unrelated Russian MPS II patients. Hum Genet
1998;103:732-5.
15. Vafiadaki E, Cooper A, Heptinstall LE, Hatton CE, Thornley M, Wraith JE. Mutation analysis in 57 unrelated patients with MPS II (Hunter's disease). Arch Dis Child 1998;79:237-41.
16. Li P, Bellows AB, Thompson JN. Molecular basis of iduronate 2-sulfatase gene mutations in patients with mucopolysaccharidosis type II (Hunter syndrome). J Med Genet 1999;36:21-7.
17. Vallance HO, Bernard L, Rashed M, Chiu D, Le G, Toone J et al. Identification of 6 novel mutation in the iduronate sulfatase gene. Mutation in brief 233. Online. Hum Mutat 1999;13:338.
18. Cudry S, Tigaud I, Froissart R, Bonnet V, Maire I, Bozon D. MPS II in females: Molecular basis of two different cases. J Med Genet 2000;37:E29.
19. Bonuccelli G, Di Natale P, Corsolini F, Villani G, Regis S, Filocamo M. The effect of four mutations on the expression of iduronate-2-sulfatase in mucopolysaccharidosis type II. Biochem Biophys Acta 2001;1537:233-8.
20. Filocamo M, Bonuccelli G, Corsolini F, Mazzotti R, Cusano R, Gatti R. Molecular analysis of 40 Italian patients with mucopolysaccharidosis type II: New mutation in the iduronate-2-sulfatase (IDS) gene. Hum Mutat 2001;21:164-5.
21. Moreira da Silva I, Froissart R, Marques dos Santos H, Caseiro C, Maire I, Bozon D. Molecular basis of mucopolysaccharidosis type II in Portugal: Identification of four novel mutations. Clin Genet 2001;60:316-8.
22. Ricci V, Regis S, Di Duca M, Filocamo M. An Alumediated rearrangement as cause of exon skipping in Hunter disease. Hum Genet 2003;112:419-25.
23. Kim CH, Hwang HZ, Song SM, Paik KH, Kwon EK, Moon KB et al. Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: Identification of 13 novel mutations. Hum Mutat 2003;21:449-50.
24. Tomatsu S, Orii KO, Bi Y, Gutierrez MA, Nishioka T, Yamaguchi S et al. General implications for CpG hot spot mutations: methylation patterns of the human iduronate-2-sulfatase gene locus. Hum Mutat 2004;23:590-8.
25. Parkinson EJ, Muller V, Hopwood JJ, Brooks DA. Iduronate 2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients. Mol Genet Metab 2004;81:58-64.
26. Chang JH, Lin SP, Lin SC, Tseng KL, Li CL, Chuang CK et al. Expression studies of mutations underlying Taiwanese Hunter syndrome (mucopolysaccharidosis type II). Hum Genet 2005;116:160-6.
27. Tomatsu S, Sukegawa K, Trandafirescu GG, Gutierrez MA, Nishioka T, Yamaguchi S et al. Differences in methylation patterns in the methylation boundary region of IDS gene in Hunter syndrome patients: implications for CpG hot spot mutations. Eur J Hum Genet 2006;14:838-45.
28. Wilson PJ, Morris CP, Anson DS, Occhiodoro T, Bielick J, Clements PR et al. Hunter syndrome: Isolation of an Iduronate 2-sulfatase cDNA clone and analysis of patients DNA. Proc Natl Acad Sci USA
1990;87:8531-5.
29. Wilson PJ, Meaney CA, Hopwood JJ, Morris CP. Sequence of the human iduronate 2-sulfatase (IDS) gene. Genomics 1993;17:773-5.
30. Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins M, Appel R et al. Protein identification and analysis tools on the expasy server. En: Walker JM, editor. The proteomics protocols handbook. New York, USA: Human Press; 2005. p.571-660.
31. Bjellqvist B, Hughes GJ, Pasquali C, Paquet N, Ravier F, Sánchez JC et al. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 1993;14:1023-31.
32. Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999;294:1351-62.
33. Julenius K, Molgaard G, Gupta R, Brunak S. Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 2005;15:153-64.
34. Blon N, Ponten T, Gupta R, Brunak S. Prediction of post-translational glycosilation and phosphorylation of proteins from aminoacid sequence. Proteomics 2004;4:1633-49.
35. Frith MC, Spoge JL, Hansen U, Weng Z. Statistical significance of clusters of motifs represented by position specific scoring matrices in nucleotide sequences. Nucleic Acids Res 2002;30:3214-24.
36. Hopp TP, Woods KR. Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci USA 1981;78:3824-8.
37. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W et al. Gapped Blast and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 1997;25:3389-402.
38. Kneller DG, Cohen FE, Langridge R. Improvements in protein secondary structure prediction by an enhanced neural network. J Mol Biol 1990;214:171-82.
39. Garnier J, Gibrat J, Robson B, Doolittle R. Gor secondary structure prediction method version iv. Methods Enzymol 1996;266:540-53.
40. Guex N, Peitisch M. SWISS-MODEL and the Swiss- PdbViewer: An environment for comparative protein modeling. Electrophoresis 1997;18:2714-23.
41. Cuff JA, Clamp ME, Siddiqui AS, Finlay M, Barton GJ. JPred: A consensus secondary structure prediction server. Bioinformatics 1998;14:892-3.
42. Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292:195-202.
43. Shindyalov IN, Bourne PE. A database and tools for 3-D protein structure comparison and alignment using the Combinatorial Extension (CE) algorithm. Nucleic Acids Res 2001:29:228-9.
44. Pollastri G, Przybylski D, Rost B, Baldi P. Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 2002;47:228-35.
45. Muñoz V, Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J Mol Biol 1994;245:275-96.
46. Combet C, Jambon M, Deléage G, Geourjon C. Geno3d: Automatic comparative molecular modeling of protein. Bioinformatics 2002;18:213-4.
47. Lambert C, Leonard N, De Bolle X, Depiereux E. ESyPred3d: Prediction of proteins 3D structures. Bioinformatics 2002;18:1250-6.
48. Discover©. Accelrys software Inc. San Diego, USA: Accelrys software Inc; 2001-2006.
49. Sayle RA, Milner-White EJ. RASMOL: Biomolecular graphics for all. Trends Biochem Sci 1995;20:374.
50. Schmidt B, Selmer T, Ingendoh A, von Figura K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency cell. Cell 1995;82:271-8.
51. Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ et al. Structure of human lysosomal sulfatase. Structure 1997;5:277-89.
52. Parenti G, Meroni G, Ballabio A. The sulfatase gene family. Curr Opin Genet Dev 1997;7:386-91.
53. Dierks T, Lecca M, Schlotterhose P, Schmidt B, von Figura K. Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases. EMBO J 1999;18:2084-91.
54. Waldow A, Schmidt B, Dierks T, Von Bulow R, von Figura K. Amino acid residues forming the active site of arylsulfatase A. Role in catalytic activity and substrate binding. J Biol Chem 1999;274:12284-8.
55. Web Lab Viewer Pro. Web Lab, Molecular Simulation. Getting Starting. Ca, USA: Web Lab Viewer Pro; 2000.
56. Baker D, Sali A. Protein structure prediction and structural genomics. Science 2001;294:93-6.
57. Chothia C, Lesk AM. The relation between the divergence of sequence and structure in proteins. EMBO J 1986;5:823-6.
58. Stemberg M. Protein structure prediction. Oxford: IRL Press; 1996. p.298.
59. Froissart R, Millat G, Mathiu M, Bozon D, Maire I. Processing of iduronate 2-sulfatase in human fibroblasts. Biochem J 1995;309:425-30.
60. Millat G, Froissart R, Maire I, Bozon D. Characterization of iduronate sulfate sulfatase mutants affecting N-glycosylations sites and cysteine-84 residue. Biochem J 1997;326:243-7.
61. Millat G, Froissart R, Maire I, Bozon D. IDS transfer from overexpressing cell to IDS-deficient. Exp Cell Res 1997;230:362-7.
62. Sosa A, Barrera L. Production of specific chicken egg yolk antibodies to Iduronate 2-sulphate sulphatase (IDS) and its applicability in an Enzime-Linked Immunosorbent Assay (Elisa). J Inherit Metab Dis 2005;28(Suppl.1);185.
63. Sáenz H. Expresión, purificación parcial y estudios computacionales de la IDShr producida en Pichia pastoris. (Tesis Doctoral). Bogotá D.C.: Facultad de Ciencias, Pontificia Universidad Javeriana; 2005. p.149.
How to Cite
1.
Sáenz H, Lareo L, Poutou RA, Sosa Ángela C, Barrera LA. Computational prediction of the tertiary structure of the human iduronate 2-sulfate sulfatase. biomedica [Internet]. 2007 Mar. 1 [cited 2024 May 19];27(1):7-20. Available from: https://revistabiomedica.org/index.php/biomedica/article/view/229
Published
2007-03-01
Issue
Section
Original articles
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