Bound water at protein-protein interfaces: partners, roles and hydrophobic bubbles as a conserved motif.

ABSTRACT:

Background

There is a great interest in understanding and exploiting protein-protein associations as new routes for treating human disease. However, these associations are difficult to structurally characterize or model although the number of X-ray structures for protein-protein complexes is expanding. One feature of these complexes that has received little attention is the role of water molecules in the interfacial region.

Methodology

A data set of 4741 water molecules abstracted from 179 high-resolution (≤ 2.30 Å) X-ray crystal structures of protein-protein complexes was analyzed with a suite of modeling tools based on the HINT forcefield and hydrogen-bonding geometry. A metric termed Relevance was used to classify the general roles of the water molecules.

Results

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SUBMITTER: Ahmed MH 

PROVIDER: S-EPMC3178540 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature