1dzi

From Proteopedia

(Difference between revisions)

Revision as of 23:35, 24 December 2014

INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX

Structural highlights

1dzi is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:	,
Related:	1aox
Resources:	FirstGlance, OCA, RCSB, PDBsum

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. Structural basis of collagen recognition by integrin alpha2beta1. Cell. 2000 Mar 31;101(1):47-56. PMID:10778855 doi:10.1016/S0092-8674(00)80622-4

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dzi"

@@ Line 8: / Line 8: @@
 <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://www.rcsb.org/pdb/explore.do?structureId=1dzi RCSB], [http://www.ebi.ac.uk/pdbsum/1dzi PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1dzi

From Proteopedia

Revision as of 23:35, 24 December 2014

INTEGRIN ALPHA2 I DOMAIN / COLLAGEN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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