Structural Basis of Mucopolysaccharidosis Type II and Construction of a Database of Mutant Iduronate 2-Sulfatases
Mucopolysaccharidosis type II (MPS II, Hunter syndrome) is an X-linked genetic disorder caused by a deficiency of iduronate 2-sulfatase (IDS), and missense mutations comprising about 30% of the mutations responsible for MPS II result in heterogeneous phenotypes ranging from the severe to the attenua...
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| creator | Saito, Seiji Ohno, Kazuki Okuyama, Torayuki Sakuraba, Hitoshi |
| description | Mucopolysaccharidosis type II (MPS II, Hunter syndrome) is an X-linked genetic disorder caused by a deficiency of iduronate 2-sulfatase (IDS), and missense mutations comprising about 30% of the mutations responsible for MPS II result in heterogeneous phenotypes ranging from the severe to the attenuated form. To elucidate the basis of MPS II from the structural viewpoint, we built structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations (phenotypes: 67 severe and 64 attenuated), and analyzed the influence of each amino acid substitution on the IDS structure by calculating the accessible surface area, the number of atoms affected and the root-mean-square distance. The results revealed that the amino acid substitutions causing MPS II were widely spread over the enzyme molecule and that the structural changes of the enzyme protein were generally larger in the severe group than in the attenuated one. Coloring of the atoms influenced by different amino acid substitutions at the same residue showed that the structural changes influenced the disease progression. Based on these data, we constructed a database of IDS mutations as to the structures of mutant IDS proteins. |
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To elucidate the basis of MPS II from the structural viewpoint, we built structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations (phenotypes: 67 severe and 64 attenuated), and analyzed the influence of each amino acid substitution on the IDS structure by calculating the accessible surface area, the number of atoms affected and the root-mean-square distance. The results revealed that the amino acid substitutions causing MPS II were widely spread over the enzyme molecule and that the structural changes of the enzyme protein were generally larger in the severe group than in the attenuated one. Coloring of the atoms influenced by different amino acid substitutions at the same residue showed that the structural changes influenced the disease progression. Based on these data, we constructed a database of IDS mutations as to the structures of mutant IDS proteins.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0163964</identifier><identifier>PMID: 27695081</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Algorithms ; Amino Acid Substitution ; Amino acids ; Analysis ; Atomic properties ; Atomic structure ; Attenuation ; Biology and Life Sciences ; Catalytic Domain ; Coloring ; Construction ; Crystal structure ; Databases, Nucleic Acid ; Development and progression ; Enzymes ; Genetic disorders ; Glycoproteins - genetics ; Heparan sulfate ; Humans ; Metabolic disorders ; Missense mutation ; Models, Molecular ; Mucopolysaccharidoses ; Mucopolysaccharidosis ; Mucopolysaccharidosis II - diagnosis ; Mucopolysaccharidosis II - genetics ; Mutation ; Mutation, Missense ; Phenotype ; Physical Sciences ; Protein Conformation ; Proteins ; Research and Analysis Methods ; Structural models ; Structure-Activity Relationship ; Studies</subject><ispartof>PloS one, 2016-10, Vol.11 (10), p.e0163964-e0163964</ispartof><rights>COPYRIGHT 2016 Public Library of Science</rights><rights>2016 Saito et al. 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To elucidate the basis of MPS II from the structural viewpoint, we built structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations (phenotypes: 67 severe and 64 attenuated), and analyzed the influence of each amino acid substitution on the IDS structure by calculating the accessible surface area, the number of atoms affected and the root-mean-square distance. The results revealed that the amino acid substitutions causing MPS II were widely spread over the enzyme molecule and that the structural changes of the enzyme protein were generally larger in the severe group than in the attenuated one. Coloring of the atoms influenced by different amino acid substitutions at the same residue showed that the structural changes influenced the disease progression. Based on these data, we constructed a database of IDS mutations as to the structures of mutant IDS proteins.</description><subject>Acids</subject><subject>Algorithms</subject><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Analysis</subject><subject>Atomic properties</subject><subject>Atomic structure</subject><subject>Attenuation</subject><subject>Biology and Life Sciences</subject><subject>Catalytic Domain</subject><subject>Coloring</subject><subject>Construction</subject><subject>Crystal structure</subject><subject>Databases, Nucleic Acid</subject><subject>Development and progression</subject><subject>Enzymes</subject><subject>Genetic disorders</subject><subject>Glycoproteins - genetics</subject><subject>Heparan sulfate</subject><subject>Humans</subject><subject>Metabolic disorders</subject><subject>Missense mutation</subject><subject>Models, Molecular</subject><subject>Mucopolysaccharidoses</subject><subject>Mucopolysaccharidosis</subject><subject>Mucopolysaccharidosis II - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saito, Seiji</au><au>Ohno, Kazuki</au><au>Okuyama, Torayuki</au><au>Sakuraba, Hitoshi</au><au>Grosso, Michela</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Basis of Mucopolysaccharidosis Type II and Construction of a Database of Mutant Iduronate 2-Sulfatases</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2016-10-03</date><risdate>2016</risdate><volume>11</volume><issue>10</issue><spage>e0163964</spage><epage>e0163964</epage><pages>e0163964-e0163964</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Mucopolysaccharidosis type II (MPS II, Hunter syndrome) is an X-linked genetic disorder caused by a deficiency of iduronate 2-sulfatase (IDS), and missense mutations comprising about 30% of the mutations responsible for MPS II result in heterogeneous phenotypes ranging from the severe to the attenuated form. To elucidate the basis of MPS II from the structural viewpoint, we built structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations (phenotypes: 67 severe and 64 attenuated), and analyzed the influence of each amino acid substitution on the IDS structure by calculating the accessible surface area, the number of atoms affected and the root-mean-square distance. The results revealed that the amino acid substitutions causing MPS II were widely spread over the enzyme molecule and that the structural changes of the enzyme protein were generally larger in the severe group than in the attenuated one. Coloring of the atoms influenced by different amino acid substitutions at the same residue showed that the structural changes influenced the disease progression. Based on these data, we constructed a database of IDS mutations as to the structures of mutant IDS proteins.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>27695081</pmid><doi>10.1371/journal.pone.0163964</doi><tpages>e0163964</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acids Algorithms Amino Acid Substitution Amino acids Analysis Atomic properties Atomic structure Attenuation Biology and Life Sciences Catalytic Domain Coloring Construction Crystal structure Databases, Nucleic Acid Development and progression Enzymes Genetic disorders Glycoproteins - genetics Heparan sulfate Humans Metabolic disorders Missense mutation Models, Molecular Mucopolysaccharidoses Mucopolysaccharidosis Mucopolysaccharidosis II - diagnosis Mucopolysaccharidosis II - genetics Mutation Mutation, Missense Phenotype Physical Sciences Protein Conformation Proteins Research and Analysis Methods Structural models Structure-Activity Relationship Studies |
| title | Structural Basis of Mucopolysaccharidosis Type II and Construction of a Database of Mutant Iduronate 2-Sulfatases |
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