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First- and second-shell metal binding residues in human proteins are disproportionately associated with disease-related SNPs
Human mutation, 2011-11, Vol.32 (11), p.1309-1318
Levy, Ronen
Sobolev, Vladimir
Edelman, Marvin
2011
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Levy, Ronen
Sobolev, Vladimir
Edelman, Marvin
Titel
First- and second-shell metal binding residues in human proteins are disproportionately associated with disease-related SNPs
Ist Teil von
Human mutation, 2011-11, Vol.32 (11), p.1309-1318
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2011
Quelle
Wiley Online Library - AutoHoldings Journals
Beschreibungen/Notizen
Protein structure serves as a key determinant for revealing the molecular basis of human disease. Metal ions are among the most frequently bound heterogroups in proteins affecting structure and function. We analyzed the relationship between single nucleotide polymorphisms (SNPs) associated with human disease and metal binding sites in proteins on a database scale, using structural models and predictive tools. A match was identified for 586 disease‐associated SNPs (dSNPs) located at 135 predicted metal binding sites and associated with 126 diverse diseases. For 104 diseases, a metal is known to bind at the predicted site in the homologue; for 22, the analysis gives a first indication for metal involvement in the disease. As second‐shell residues play an important part in metal ion binding, our analysis included protein space up to 4.5 Å from metal binding sites. The ratio of disease‐associated versus nondisease‐associated SNPs (dSNP/ndSNP) for first‐shell residues is 7.4 and for second‐shell residues, 3.1. In addition, over 13% of all dSNPs were found to be associated with first‐ and second‐shell residues, although these residues occupy only about 3% of protein space. These results show a disproportionate association of dSNPs and metal binding sites over a wide variety of diseases. Hum Mutat 32:1309–1318, 2011. ©2011 Wiley Periodicals, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 1059-7794, 1098-1004
eISSN: 1098-1004
DOI: 10.1002/humu.21573
Titel-ID: cdi_proquest_miscellaneous_899131556
Format
–
Schlagworte
Binding Sites
,
functional annotation
,
Genetic Predisposition to Disease
,
human disease
,
Humans
,
Ions
,
metal binding sites
,
Metals
,
Metals - metabolism
,
Models, Molecular
,
Polymorphism, Single Nucleotide
,
protein modeling
,
Protein structure
,
Proteins - chemistry
,
Proteins - metabolism
,
Single-nucleotide polymorphism
,
SNP
,
Structure-function relationships
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