Correlated mutation analysis on the catalytic domains of serine/threonine protein kinases.

ABSTRACT:

Background

Protein kinases (PKs) have emerged as the largest family of signaling proteins in eukaryotic cells and are involved in every aspect of cellular regulation. Great progresses have been made in understanding the mechanisms of PKs phosphorylating their substrates, but the detailed mechanisms, by which PKs ensure their substrate specificity with their structurally conserved catalytic domains, still have not been adequately understood. Correlated mutation analysis based on large sets of diverse sequence data may provide new insights into this question.

Methodology/principal findings

Statistical coupling, residue correlation and mutual information analyses along with clustering were applied to analyze the structure-based multiple sequence alignment of the catalytic domai

SUBMITTER: Xu F 

PROVIDER: S-EPMC2690836 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature