2z4f
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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.
DiseaseDisease
Known disease associated with this structure: Wernicke-Korsakoff syndrome, susceptibility to OMIM:[606781]
About this StructureAbout 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.
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 Aug 16;. PMID:17703188
Page seeded by OCA on Mon Nov 12 23:46:50 2007