Small-molecule inhibitor starting points learned from protein-protein interaction inhibitor structure.

ABSTRACT:

Motivation

Protein-protein interactions (PPIs) are a promising, but challenging target for pharmaceutical intervention. One approach for addressing these difficult targets is the rational design of small-molecule inhibitors that mimic the chemical and physical properties of small clusters of key residues at the protein-protein interface. The identification of appropriate clusters of interface residues provides starting points for inhibitor design and supports an overall assessment of the susceptibility of PPIs to small-molecule inhibition.

Results

We extract Small-Molecule Inhibitor Starting Points (SMISPs) from protein-ligand and protein-protein complexes in the Protein Data Bank (PDB). These SMISPs are used to train two distinct classifiers, a support vector machine and an

SUBMITTER: Koes DR 

PROVIDER: S-EPMC3307105 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature