Structure-guided selection of specificity determining positions in the human Kinome.

ABSTRACT:

Background

The human kinome contains many important drug targets. It is well-known that inhibitors of protein kinases bind with very different selectivity profiles. This is also the case for inhibitors of many other protein families. The increased availability of protein 3D structures has provided much information on the structural variation within a given protein family. However, the relationship between structural variations and binding specificity is complex and incompletely understood. We have developed a structural bioinformatics approach which provides an analysis of key determinants of binding selectivity as a tool to enhance the rational design of drugs with a specific selectivity profile.

Results

We propose a greedy algorithm that computes a subset of residue positi

SUBMITTER: Moll M 

PROVIDER: S-EPMC5001202 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature