Detecting protein kinase recognition modes of calmodulin by residual dipolar coupling
 

Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.

Related Articles Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.

Biochemistry. 2002 Oct 29;41(43):12899-906

Authors: Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M

Calmodulin-regulated serine/threonine kinases (CaM kinases) play crucial roles in Ca2+-dependent signaling transduction pathways in eukaryotes. Despite having a similar overall molecular architecture of catalytic and regulatory domains, CaM kinases employ different binding modes for Ca2+/CaM recruitment which is required for their activation. Here we present a residual dipolar coupling (RDC)-based NMR approach to characterizing the molecular recognition of CaM with five different CaM kinases. Our analyses indicate that CaM kinase I and likely IV use the same CaM binding mode as myosin light chain kinase (1-14 motif), distinct from those of CaM kinase II (1-10 motif) and CaM kinase kinase (1-16- motif). This NMR approach provides an efficient experimental guide for homology modeling and structural characterization of CaM-target complexes.

PMID: 12390014 [PubMed - indexed for MEDLINE]



Source: PubMed