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[[Image:1dgu.jpg|left|200px]]<br /><applet load="1dgu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dgu" />
'''HOMOLOGY-BASED MODEL OF CALCIUM-SATURATED CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)'''<br />


==Overview==
==HOMOLOGY-BASED MODEL OF CALCIUM-SATURATED CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)==
Calcium- and integrin-binding protein (CIB) binds to the 20-residue, alphaIIb cytoplasmic domain of platelet alphaIIbbeta3 integrin. Amino acid, sequence similarities with calmodulin (CaM) and calcineurin B (CnB), allowed the construction of homology-based models of calcium-saturated CIB, as well as apo-CIB. In addition, the solution structure of the alphaIIb, cytoplasmic domain in 45% aqueous trifluoroethanol was solved by, conventional two-dimensional NMR methods. The models indicate that the, N-terminal domain of CIB possesses a number of positively charged residues, in its binding site that could interact with the acidic carboxy-terminal, LEEDDEEGE sequence of alphaIIb. The C-terminal domain of CIB seems, well-suited to bind the sequence WKVGFFKR, which forms a well-structured, alpha helix; this is analogous to calmodulin and calcineurin B, which also, bind alpha helices. Similarities between the C-terminal domains of CIB and, calmodulin suggest that binding of CIB to the cytoplasmic domain of, alphaIIb may be affected by fluctuations in the intracellular calcium, concentration.
<StructureSection load='1dgu' size='340' side='right'caption='[[1dgu]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dgu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DGU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgu OCA], [https://pdbe.org/1dgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dgu RCSB], [https://www.ebi.ac.uk/pdbsum/1dgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dgu ProSAT]</span></td></tr>
</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/dg/1dgu_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=1dgu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calcium- and integrin-binding protein (CIB) binds to the 20-residue alphaIIb cytoplasmic domain of platelet alphaIIbbeta3 integrin. Amino acid sequence similarities with calmodulin (CaM) and calcineurin B (CnB) allowed the construction of homology-based models of calcium-saturated CIB as well as apo-CIB. In addition, the solution structure of the alphaIIb cytoplasmic domain in 45% aqueous trifluoroethanol was solved by conventional two-dimensional NMR methods. The models indicate that the N-terminal domain of CIB possesses a number of positively charged residues in its binding site that could interact with the acidic carboxy-terminal LEEDDEEGE sequence of alphaIIb. The C-terminal domain of CIB seems well-suited to bind the sequence WKVGFFKR, which forms a well-structured alpha helix; this is analogous to calmodulin and calcineurin B, which also bind alpha helices. Similarities between the C-terminal domains of CIB and calmodulin suggest that binding of CIB to the cytoplasmic domain of alphaIIb may be affected by fluctuations in the intracellular calcium concentration.


==Disease==
Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies.,Hwang PM, Vogel HJ J Mol Recognit. 2000 Mar-Apr;13(2):83-92. PMID:10822252<ref>PMID:10822252</ref>
Known disease associated with this structure: Multiple endocrine neoplasia, type IV OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600778 600778]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1DGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGU OCA].
</div>
 
<div class="pdbe-citations 1dgu" style="background-color:#fffaf0;"></div>
==Reference==
== References ==
Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies., Hwang PM, Vogel HJ, J Mol Recognit. 2000 Mar-Apr;13(2):83-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10822252 10822252]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hwang, P.M.]]
[[Category: Hwang PM]]
[[Category: Vogel, H.J.]]
[[Category: Vogel HJ]]
[[Category: blood clotting]]
[[Category: ef-hands]]
[[Category: helical]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:39:49 2008''

Latest revision as of 08:24, 22 May 2024

HOMOLOGY-BASED MODEL OF CALCIUM-SATURATED CIB (CALCIUM-AND INTEGRIN-BINDING PROTEIN)

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