1dzi: Difference between revisions

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New page: left|200px<br /> <applet load="1dzi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dzi, resolution 2.1Å" /> '''INTEGRIN ALPHA2 I DO...
 
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[[Image:1dzi.gif|left|200px]]<br />
[[Image:1dzi.gif|left|200px]]<br /><applet load="1dzi" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1dzi" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1dzi, resolution 2.1&Aring;" />
caption="1dzi, resolution 2.1&Aring;" />
'''INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX'''<br />
'''INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX'''<br />


==Overview==
==Overview==
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.
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.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1DZI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CO and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZI OCA].  
1DZI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZI OCA].  


==Reference==
==Reference==
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[[Category: integrin]]
[[Category: integrin]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:08 2008''