1dzi: Difference between revisions
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|PDB= 1dzi |SIZE=350|CAPTION= <scene name='initialview01'>1dzi</scene>, resolution 2.1Å | |PDB= 1dzi |SIZE=350|CAPTION= <scene name='initialview01'>1dzi</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> | |LIGAND= <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> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1dzi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dzi RCSB]</span> | |||
}} | }} | ||
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==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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Knight, G.]] | [[Category: Knight, G.]] | ||
[[Category: Liddington, R.]] | [[Category: Liddington, R.]] | ||
[[Category: collagen]] | [[Category: collagen]] | ||
[[Category: integrin]] | [[Category: integrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:51:53 2008'' | ||