1dzi: Difference between revisions

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{{Seed}}
[[Image:1dzi.png|left|200px]]


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==integrin alpha2 I domain / collagen complex==
The line below this paragraph, containing "STRUCTURE_1dzi", creates the "Structure Box" on the page.
<StructureSection load='1dzi' size='340' side='right'caption='[[1dzi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dzi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1DZI FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
{{STRUCTURE_1dzi|  PDB=1dzi  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzi OCA], [https://pdbe.org/1dzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzi RCSB], [https://www.ebi.ac.uk/pdbsum/1dzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzi ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
== 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/dz/1dzi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1dzi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX===
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>
</div>
<div class="pdbe-citations 1dzi" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_10778855}}, adds the Publication Abstract to the page
*[[Collagen 3D structures|Collagen 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10778855 is the PubMed ID number.
*[[Integrin 3D structures|Integrin 3D structures]]
-->
== References ==
{{ABSTRACT_PUBMED_10778855}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
1DZI is a [[Protein complex]] structure of sequences 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=1DZI OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10778855 10778855]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Barnes, M.]]
[[Category: Synthetic construct]]
[[Category: Emsley, J.]]
[[Category: Barnes M]]
[[Category: Farndale, R.]]
[[Category: Emsley j]]
[[Category: Knight, G.]]
[[Category: Farndale R]]
[[Category: Liddington, R.]]
[[Category: Knight G]]
[[Category: Collagen]]
[[Category: Liddington R]]
[[Category: Integrin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:53:31 2008''

Latest revision as of 08:17, 9 April 2025

integrin alpha2 I domain / collagen complex

1dzi, resolution 2.10Å

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