Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.

Abstract excerpt

We have carried out a thorough and systematic sequence-structure study on how the pattern of conservation at the interface differs from the noninteracting surface in seven proteases and their inhibitors. As expected, the interface of a protease could be easily distinguished from the noninteracting surface by a concentrated area of conservation. In contrast, there was less distinction to be made between the...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Algorithms
• Share to Databases as Topic
• Share to Endopeptidases