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2z4f
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase | + | 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. |
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| + | ==Disease== | ||
| + | Known disease associated with this structure: Wernicke-Korsakoff syndrome, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606781 606781]] | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==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 Aug 16 | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17703188 17703188] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Receptor protein-tyrosine kinase]] | [[Category: Receptor protein-tyrosine kinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:05 2008'' |
Revision as of 17:00, 21 February 2008
|
Solution structure of the Discoidin Domain of DDR2
Contents |
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.
Disease
Known disease associated with this structure: Wernicke-Korsakoff syndrome, susceptibility to OMIM:[606781]
About this Structure
2Z4F is a Single protein structure of sequence from Homo sapiens. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 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 Thu Feb 21 19:00:05 2008
