Lessons in Protein Design from Combined Evolution and Conformational Dynamics.

ABSTRACT: Protein-protein interactions play important roles in the control of every cellular process. How natural selection has optimized protein design to produce molecules capable of binding to many partner proteins is a fascinating problem but not well understood. Here, we performed a combinatorial analysis of protein sequence evolution and conformational dynamics to study how calmodulin (CaM), which plays essential roles in calcium signaling pathways, has adapted to bind to a large number of partner proteins. We discovered that amino acid residues in CaM can be partitioned into unique classes according to their degree of evolutionary conservation and local stability. Holistically, categorization of CaM residues into these classes reveals enriched physico-chemical interactions required for bindin

SUBMITTER: Tripathi S 

PROVIDER: S-EPMC4585694 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature