1xo5: Difference between revisions
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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== | ||
<StructureSection load='1xo5' size='340' side='right' caption='[[1xo5]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='1xo5' size='340' side='right' caption='[[1xo5]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xo5]] is a 2 chain structure | <table><tr><td colspan='2'>[[1xo5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XO5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo5 OCA], [http://pdbe.org/1xo5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xo5 RCSB], [http://www.ebi.ac.uk/pdbsum/1xo5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xo5 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo5 OCA], [http://pdbe.org/1xo5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xo5 RCSB], [http://www.ebi.ac.uk/pdbsum/1xo5 PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Betts, L]] | [[Category: Betts, L]] | ||
[[Category: Ferrara, J D]] | [[Category: Ferrara, J D]] | ||
Revision as of 10:00, 5 April 2017
Crystal structure of CIB1, an EF-hand, integrin and kinase-binding proteinCrystal structure of CIB1, an EF-hand, integrin and kinase-binding protein
Structural highlights
Function[CIB1_HUMAN] May convert the inactive conformation of integrin alpha-IIb/beta3 to an active form through binding to the integrin cytoplasmic domain. Induces cell migration and spreading mediated through integrin (possibly via focal adhesion complexes). Functions as a negative regulator of stress activated MAP kinase (MAPK) signaling pathways. May play a role in regulation of apoptosis. Interacts with and up-regulates PTK2/FAK1 activity. Down regulates inositol 1,4,5-trisphosphate receptor-dependent calcium signaling. Participates in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation.[1] [2] [3] [4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCIB1 (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. 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[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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