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| - | [[Image:1y1a.gif|left|200px]]<br /> | |
| - | <applet load="1y1a" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1y1a, resolution 2.30Å" /> | |
| - | '''CRYSTAL STRUCTURE OF CALCIUM AND INTEGRIN BINDING PROTEIN'''<br /> | |
| | | | |
| - | ==Overview== | + | ==CRYSTAL STRUCTURE OF CALCIUM AND INTEGRIN BINDING PROTEIN== |
| - | Calcium- and integrin-binding protein 1 (CIB1) is involved in the process, of platelet aggregation by binding the cytoplasmic tail of the alpha(IIb), subunit of the platelet-specific integrin alpha(Iib)beta(3). Although, poorly understood, it is widely believed that CIB1 acts as a global, signaling regulator because it is expressed in many tissues that do not, express integrin alpha(Iib)beta(3). We report the structure of human CIB1, to a resolution of 2.3 A, crystallized as a dimer. The dimer interface, includes an extensive hydrophobic patch in a crystal form with 80% solvent, content. Although the dimer form of CIB1 may not be physiologically, relevant, this intersub-unit surface is likely to be linked to alpha(IIb), binding and to the binding of other signaling partner proteins. The, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15840829 (full description)]]
| + | <StructureSection load='1y1a' size='340' side='right'caption='[[1y1a]], [[Resolution|resolution]] 2.30Å' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <table><tr><td colspan='2'>[[1y1a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1A FirstGlance]. <br> |
| - | 1Y1A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and GSH as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: CA1, CA2, CA3 and CA4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y1A OCA]]. | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | ==Reference== | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1a OCA], [https://pdbe.org/1y1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1a RCSB], [https://www.ebi.ac.uk/pdbsum/1y1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1a ProSAT]</span></td></tr> |
| - | The crystal structure of calcium- and integrin-binding protein 1: insights into redox regulated functions., Blamey CJ, Ceccarelli C, Naik UP, Bahnson BJ, Protein Sci. 2005 May;14(5):1214-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15840829 15840829]
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CIB1_HUMAN 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.<ref>PMID:12714504</ref> <ref>PMID:12881299</ref> <ref>PMID:15685448</ref> <ref>PMID:18627437</ref> <ref>PMID:19805025</ref> <ref>PMID:21264284</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y1/1y1a_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y1a ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Bahnson, B.J.]] | + | [[Category: Bahnson BJ]] |
| - | [[Category: Blamey, C.J.]] | + | [[Category: Blamey CJ]] |
| - | [[Category: Ceccarelli, C.]] | + | [[Category: Ceccarelli C]] |
| - | [[Category: Naik, U.P.]] | + | [[Category: Naik UP]] |
| - | [[Category: CA]]
| + | |
| - | [[Category: GSH]]
| + | |
| - | [[Category: calcium]]
| + | |
| - | [[Category: calcium-binding protein]]
| + | |
| - | [[Category: ef-hand]]
| + | |
| - | [[Category: glutathiolation]]
| + | |
| - | [[Category: glutathione]]
| + | |
| - | [[Category: integrin]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:17:19 2007''
| + | |
| 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.
References
- ↑ Naik UP, Naik MU. Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen. Blood. 2003 Aug 15;102(4):1355-62. Epub 2003 Apr 24. PMID:12714504 doi:10.1182/blood-2003-02-0591
- ↑ Naik MU, Naik UP. Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen. Blood. 2003 Nov 15;102(10):3629-36. Epub 2003 Jul 24. PMID:12881299 doi:10.1182/blood-2003-05-1703
- ↑ Tahara E Jr, Tahara H, Kanno M, Naka K, Takeda Y, Matsuzaki T, Yamazaki R, Ishihara H, Yasui W, Barrett JC, Ide T, Tahara E. G1P3, an interferon inducible gene 6-16, is expressed in gastric cancers and inhibits mitochondrial-mediated apoptosis in gastric cancer cell line TMK-1 cell. Cancer Immunol Immunother. 2005 Aug;54(8):729-40. Epub 2005 Feb 1. PMID:15685448 doi:10.1007/s00262-004-0645-2
- ↑ Hennigs JK, Burhenne N, Stahler F, Winnig M, Walter B, Meyerhof W, Schmale H. Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP3-dependent Ca2+ release in vivo. J Neurochem. 2008 Sep;106(5):2249-62. doi: 10.1111/j.1471-4159.2008.05563.x. PMID:18627437 doi:10.1111/j.1471-4159.2008.05563.x
- ↑ Yoon KW, Cho JH, Lee JK, Kang YH, Chae JS, Kim YM, Kim J, Kim EK, Kim SE, Baik JH, Naik UP, Cho SG, Choi EJ. CIB1 functions as a Ca(2+)-sensitive modulator of stress-induced signaling by targeting ASK1. Proc Natl Acad Sci U S A. 2009 Oct 13;106(41):17389-94. doi:, 10.1073/pnas.0812259106. Epub 2009 Sep 29. PMID:19805025 doi:10.1073/pnas.0812259106
- ↑ Kostyak JC, Naik UP. Calcium- and integrin-binding protein 1 regulates endomitosis and its interaction with Polo-like kinase 3 is enhanced in endomitotic Dami cells. PLoS One. 2011 Jan 14;6(1):e14513. doi: 10.1371/journal.pone.0014513. PMID:21264284 doi:10.1371/journal.pone.0014513
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