1xo5
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Crystal structure of CIB1, an EF-hand, integrin and kinase-binding protein
OverviewOverview
CIB1 (CIB) is an EF-hand-containing protein that binds multiple effector, proteins, including the platelet alphaIIbbeta3 integrin and several, serine/threonine kinases and potentially modulates their function. The, crystal structure for Ca(2+)-bound CIB1 has been determined at 2.0 A, resolution and reveals a compact alpha-helical protein containing four, EF-hands, the last two of which bind calcium ions in the standard fashion, seen in many other EF-hand proteins. CIB1 shares high structural, similarity with calcineurin B and the neuronal calcium sensor (NCS) family, of EF-hand-containing proteins. Most importantly, like calcineurin B and, NCS proteins, which possess a large hydrophobic pocket necessary for, ligand binding, CIB1 contains a hydrophobic pocket that has been, implicated in ligand binding by previous mutational analysis. However, unlike several NCS proteins, Ca(2+)-bound CIB1 is largely monomeric, whether bound to a relevant peptide ligand or ligand-free. Differences in, structure, oligomeric state, and phylogeny define a new family of, CIB1-related proteins that extends from arthropods to humans.
DiseaseDisease
Known disease associated with this structure: Multiple endocrine neoplasia, type IV OMIM:[600778]
About this StructureAbout this Structure
1XO5 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural and biochemical characterization of CIB1 delineates a new family of EF-hand-containing proteins., Gentry HR, Singer AU, Betts L, Yang C, Ferrara JD, Sondek J, Parise LV, J Biol Chem. 2005 Mar 4;280(9):8407-15. Epub 2004 Dec 1. PMID:15574431
Page seeded by OCA on Fri Feb 15 17:09:49 2008