1dzi

==INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX==

<StructureSection load='1dzi' size='340' side='right' caption='[[1dzi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1dzi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DZI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aox|1aox]]</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=1dzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzi OCA], [http://pdbe.org/1dzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dzi RCSB], [http://www.ebi.ac.uk/pdbsum/1dzi PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ITA2_HUMAN ITA2_HUMAN]] Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dz/1dzi_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

We have determined the crystal structure of a complex between the I domain of integrin alpha2beta1 and a triple helical collagen peptide containing a critical GFOGER motif. Three loops on the upper surface of the I domain that coordinate a metal ion also engage the collagen, with a collagen glutamate completing the coordination sphere of the metal. Comparison with the unliganded I domain reveals a change in metal coordination linked to a reorganization of the upper surface that together create a complementary surface for binding collagen. Conformational changes propagate from the upper surface to the opposite pole of the domain, suggesting both a basis for affinity regulation and a pathway for signal transduction. The structural features observed here may represent a general mechanism for integrin-ligand recognition.

Structural basis of collagen recognition by integrin alpha2beta1.,Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC Cell. 2000 Mar 31;101(1):47-56. PMID:10778855<ref>PMID:10778855</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1dzi" style="background-color:#fffaf0;"></div>

*[[Collagen|Collagen]]

*[[Integrin|Integrin]]

[[Category: Human]]

[[Category: Barnes, M]]

[[Category: Emsley, J]]

[[Category: Farndale, R]]

[[Category: Knight, G]]

[[Category: Liddington, R]]

[[Category: Collagen]]

[[Category: Integrin]]