Abstract
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 β-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.
Original language | English |
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Pages (from-to) | 4168-4176 |
Number of pages | 9 |
Journal | EMBO Journal |
Volume | 26 |
Issue number | 18 |
DOIs | |
Publication status | Published - 2007 Sep 19 |
Keywords
- Collagen
- Discoidin domain receptor
- NMR
- Protein-protein interaction
- Transferred cross-saturation
ASJC Scopus subject areas
- Neuroscience(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Immunology and Microbiology(all)