1iwq
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Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this StructureAbout this Structure
1IWQ is a Protein complex structure of sequences from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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