Conformational preference of ChaK1 binding peptides: a molecular dynamics study.

ABSTRACT: TRPM7/ChaK1 is a recently discovered atypical protein kinase that has been suggested to selectively phosphorylate the substrate residues located in alpha-helices. However, the actual structure of kinase-substrate complex has not been determined experimentally and the recognition mechanism remains unknown. In this work we explored possible kinase-substrate binding modes and the likelihood of an alpha-helix docking interaction, within a kinase active site, using molecular modeling. Specifically kinase ChaK1 and its two peptide substrates were examined; one was an 11-residue segment from the N-terminal domain of annexin-1, a putative endogenous substrate for ChaK1, and the other was an engineered 16-mer peptide substrate determined via peptide library screening. Simulated annealing (SA), repl

SUBMITTER: Zhang J 

PROVIDER: S-EPMC2831825 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature