Publication: Similar binding sites and different partners: implications to shared proteins in cellular pathways
Program
KU-Authors
KU Authors
Co-Authors
Nussinov, Ruth
Publication Date
Language
Type
Embargo Status
Journal Title
Journal ISSN
Volume Title
Alternative Title
Abstract
We studied a data set of structurally similar interfaces that bind to proteins with different binding-site structures and different functions. Our multipartner protein interface clusters enable us to address questions like: What makes a given site bind different proteins? How similar/different are the interactions? And, what drives the apparently less-specific association? We find that proteins with common binding-site motifs preferentially use conserved interactions at similar interface locations, despite the different partners. Helices are major vehicles for binding different partners, allowing alternate ways to achieve favorable association. The binding sites are characterized by imperfect packing, planar architectures, bridging water molecules, and, on average, smaller size. Interestingly, analysis of the connectivity of these proteins illustrates that they have more interactions with other proteins. These findings are important in predicting "date hubs," if we assume that "date hubs" are shared proteins with binding sites capable of transient binding to multipartners, linking higher-order networks.
Source
Publisher
Cell Press
Subject
Biochemistry, Molecular biology, Biophysics, Cell biology
Citation
Has Part
Source
Structure
Book Series Title
Edition
DOI
10.1016/j.str.2007.01.007