1iwq

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1iwq, resolution 2.00Å ()
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates: save as pdb, mmCIF, xml



Contents

Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin

Publication Abstract from PubMed

The calmodulin-binding domain of myristoylated alanine-rich C kinase substrate (MARCKS), which interacts with various targets including calmodulin, actin and membrane lipids, has been suggested to function as a crosstalk point among several signal transduction pathways. We present here the crystal structure at 2 A resolution of a peptide consisting of the MARCKS calmodulin (CaM)-binding domain in complex with Ca2+-CaM. The domain assumes a flexible conformation, and the hydrophobic pocket of the calmodulin N-lobe, which is a common CaM-binding site observed in previously resolved Ca2+-CaM-target peptide complexes, is not involved in the interaction. The present structure presents a novel target-recognition mode of calmodulin and provides insight into the structural basis of the flexible interaction module of MARCKS.

Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin., Yamauchi E, Nakatsu T, Matsubara M, Kato H, Taniguchi H, Nat Struct Biol. 2003 Mar;10(3):226-31. PMID:12577052

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1iwq is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Yamauchi E, Nakatsu T, Matsubara M, Kato H, Taniguchi H. Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat Struct Biol. 2003 Mar;10(3):226-31. PMID:12577052 doi:10.1038/nsb900

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