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PMID: 17154416 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Role of intrinsic disorder in transient interactions of hub proteins.

Proteins ·Vol. 66 ·No. 4 ·2007-03-01 ·Pages 761-5

Singh GP, Ganapathi M, Dash D

Abstract

Hubs in the protein-protein interaction network have been classified as "party" hubs, which are highly correlated in their mRNA expression with their partners while "date" hubs show lesser correlation. In this study, we explored the role of intrinsic disorder in date and party hub interactions. The data reveals that intrinsic disorder is significantly enriched in date hub proteins when compared with party hub proteins. Intrinsic disorder has been largely implicated in transient binding interactions. The disorder to order transition, which occurs during binding interactions in disordered regions, renders the interaction highly reversible while maintaining the high specificity. The enrichment of intrinsic disorder in date hubs may facilitate transient interactions, which might be required for date hubs to interact with different partners at different times.

MeSH Terms
Computational Biology ELAV Proteins/chemistry,metabolism Protein Binding Protein Structure, Secondary
Chemicals
ELAV Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Singh Gajinder Pal
Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Delhi, India.
Ganapathi Mythily
Dash Debasis
Article Info
Journal
Proteins
Abbr.
Proteins
ISSN
1097-0134
Published
2007-03-01
Pages
761-5
Language
English
Region
United States
NLM ID
8700181
Subset
IM
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