Predicting protein ligand binding sites by combining evolutionary sequence conservation and 3D structure.

ABSTRACT: Identifying a protein's functional sites is an important step towards characterizing its molecular function. Numerous structure- and sequence-based methods have been developed for this problem. Here we introduce ConCavity, a small molecule binding site prediction algorithm that integrates evolutionary sequence conservation estimates with structure-based methods for identifying protein surface cavities. In large-scale testing on a diverse set of single- and multi-chain protein structures, we show that ConCavity substantially outperforms existing methods for identifying both 3D ligand binding pockets and individual ligand binding residues. As part of our testing, we perform one of the first direct comparisons of conservation-based and structure-based methods. We find that the two approaches

SUBMITTER: Capra JA 

PROVIDER: S-EPMC2777313 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature