This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2z4f
From Proteopedia
|
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 Aug 16;. PMID:17703188
Page seeded by OCA on Mon Nov 12 23:46:50 2007
