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PMID: 19594871 Published · epublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Protein disorder in the human diseasome: unfoldomics of human genetic diseases.

BMC genomics ·Vol. 10 Suppl 1 ·2009-07-07 ·Pages S12

Midic U, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN

Abstract

Intrinsically disordered proteins lack stable structure under physiological conditions, yet carry out many crucial biological functions, especially functions associated with regulation, recognition, signaling and control. Recently, human genetic diseases and related genes were organized into a bipartite graph (Goh KI, Cusick ME, Valle D, Childs B, Vidal M, et al. (2007) The human disease network. Proc Natl Acad Sci U S A 104: 8685-8690). This diseasome network revealed several significant features such as the common genetic origin of many diseases. We analyzed the abundance of intrinsic disorder in these diseasome network proteins by means of several prediction algorithms, and we analyzed the functional repertoires of these proteins based on prior studies relating disorder to function. Our analyses revealed that (i) Intrinsic disorder is common in proteins associated with many human genetic diseases; (ii) Different disease classes vary in the IDP contents of their associated proteins; (iii) Molecular recognition features, which are relatively short loosely structured protein regions within mostly disordered sequences and which gain structure upon binding to partners, are common in the diseasome, and their abundance correlates with the intrinsic disorder level; (iv) Some disease classes have a significant fraction of genes affected by alternative splicing, and the alternatively spliced regions in the corresponding proteins are predicted to be highly disordered; and (v) Correlations were found among the various diseasome graph-related properties and intrinsic disorder. These observations provide the basis for the construction of the human-genetic-disease-associated unfoldome.

MeSH Terms
Algorithms Alternative Splicing Computational Biology Databases, Protein Humans Protein Conformation Protein Folding Proteins/metabolism Proteomics Structure-Activity Relationship
Chemicals
Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Midic Uros
Center for Information Science and Technology, Temple University, Philadelphia, PA 19122, USA. uros@ist.temple.edu
Oldfield Christopher J
Dunker A Keith
Obradovic Zoran
Uversky Vladimir N
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Article Info
Journal
BMC genomics
Abbr.
BMC Genomics
ISSN
1471-2164
DOI
10.1186/1471-2164-10-S1-S12
Email
uros@ist.temple.edu
Published
2009-07-07
Epub
2009-00-07
Pages
S12
Language
English
Region
England
NLM ID
100965258
PMCID
PMC2709255
Subset
IM
Grants
NIGMS NIH HHS · R01 GM071714 · United States
NLM NIH HHS · R01 LM007688 · United States
NIGMS NIH HHS · GM071714-01A2 · United States
NLM NIH HHS · R01 LM007688-01A1 · United States
External Links
PubMed source DOI: 10.1186/1471-2164-10-S1-S12 PMC Full Text View journal details
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