1iwq
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| , resolution 2.00Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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