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| {{STRUCTURE_1xo5| PDB=1xo5 | SCENE= }} | | {{STRUCTURE_1xo5| PDB=1xo5 | SCENE= }} |
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| '''Crystal structure of CIB1, an EF-hand, integrin and kinase-binding protein'''
| | ===Crystal structure of CIB1, an EF-hand, integrin and kinase-binding protein=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15574431}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15574431 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15574431}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ef-hand]] | | [[Category: Ef-hand]] |
| [[Category: Kinase interacting protein]] | | [[Category: Kinase interacting protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:17:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:40:38 2008'' |