2z4f

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[[Image:2z4f.gif|left|200px]]
[[Image:2z4f.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2z4f |SIZE=350|CAPTION= <scene name='initialview01'>2z4f</scene>
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The line below this paragraph, containing "STRUCTURE_2z4f", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= DDR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2z4f| PDB=2z4f | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z4f OCA], [http://www.ebi.ac.uk/pdbsum/2z4f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2z4f RCSB]</span>
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'''Solution structure of the Discoidin Domain of DDR2'''
'''Solution structure of the Discoidin Domain of DDR2'''
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[[Category: Osawa, M.]]
[[Category: Osawa, M.]]
[[Category: Shimada, I.]]
[[Category: Shimada, I.]]
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[[Category: beta barrel]]
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[[Category: Beta barrel]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:56:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:18:28 2008''
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Revision as of 16:56, 4 May 2008

Image:2z4f.gif

Template:STRUCTURE 2z4f

Solution structure of the Discoidin Domain of DDR2


Overview

Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase activated by the binding of its discoidin (DS) domain to fibrillar collagen. Here, we have determined the NMR structure of the DS domain in DDR2 (DDR2-DS domain), and identified the binding site to fibrillar collagen by transferred cross-saturation experiments. The DDR2-DS domain structure adopts a distorted jellyroll fold, consisting of eight beta-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The surface profile of the collagen-binding site suggests that the DDR2-DS domain recognizes specific sites on fibrillar collagen. This study provides a molecular basis for the collagen-binding mode of the DDR2-DS domain.

About this Structure

2Z4F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of the collagen-binding mode of discoidin domain receptor 2., Ichikawa O, Osawa M, Nishida N, Goshima N, Nomura N, Shimada I, EMBO J. 2007 Sep 19;26(18):4168-76. Epub 2007 Aug 16. PMID:17703188 Page seeded by OCA on Sun May 4 19:56:24 2008

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