Global analysis of small molecule binding to related protein targets

PLoS Comput Biol. 2012 Jan;8(1):e1002333. doi: 10.1371/journal.pcbi.1002333. Epub 2012 Jan 12.

Abstract

We report on the integration of pharmacological data and homology information for a large scale analysis of small molecule binding to related targets. Differences in small molecule binding have been assessed for curated pairs of human to rat orthologs and also for recently diverged human paralogs. Our analysis shows that in general, small molecule binding is conserved for pairs of human to rat orthologs. Using statistical tests, we identified a small number of cases where small molecule binding is different between human and rat, some of which had previously been reported in the literature. Knowledge of species specific pharmacology can be advantageous for drug discovery, where rats are frequently used as a model system. For human paralogs, we demonstrate a global correlation between sequence identity and the binding of small molecules with equivalent affinity. Our findings provide an initial general model relating small molecule binding and sequence divergence, containing the foundations for a general model to anticipate and predict within-target-family selectivity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Databases, Factual
  • Drug Discovery
  • Humans
  • Ligands
  • Proteins / chemistry*
  • Proteins / metabolism
  • Rats

Substances

  • Ligands
  • Proteins