1dzi: Difference between revisions

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[[Image:1dzi.gif|left|200px]]


{{Structure
==integrin alpha2 I domain / collagen complex==
|PDB= 1dzi |SIZE=350|CAPTION= <scene name='initialview01'>1dzi</scene>, resolution 2.1&Aring;
<StructureSection load='1dzi' size='340' side='right'caption='[[1dzi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
}}
<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/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=1dzi ConSurf].
<div style="clear:both"></div>


'''INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX'''
==See Also==
 
*[[Collagen 3D structures|Collagen 3D structures]]
 
*[[Integrin 3D structures|Integrin 3D structures]]
==Overview==
__TOC__
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.
</StructureSection>
 
==Disease==
Known diseases associated with this structure: Glycoprotein Ia deficiency (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192974 192974]], Neonatal alloimmune thrombocytopenia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192974 192974]]
 
==About this Structure==
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: CO]]
[[Category: Liddington R]]
[[Category: NH2]]
[[Category: collagen]]
[[Category: integrin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:02 2008''

Latest revision as of 12:56, 20 March 2024

integrin alpha2 I domain / collagen complexintegrin alpha2 I domain / collagen complex

Structural highlights

1dzi is a 4 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1dzi, resolution 2.10Å

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