2z4f: Difference between revisions
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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.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[Category: | [[Category: Transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:56:24 2008'' | |||
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Revision as of 19:56, 4 May 2008
Solution structure of the Discoidin Domain of DDR2
OverviewOverview
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 StructureAbout this Structure
2Z4F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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