Structural basis of the collagen-binding mode of discoidin domain receptor 2

Osamu Ichikawa, Masanori Osawa, Noritaka Nishida, Naoki Goshima, Nobuo Nomura, Ichio Shimada

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84 Citations (Scopus)

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 languageEnglish
Pages (from-to)4168-4176
Number of pages9
JournalEMBO Journal
Volume26
Issue number18
DOIs
Publication statusPublished - 2007 Sep 19
Externally publishedYes

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)

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    Ichikawa, O., Osawa, M., Nishida, N., Goshima, N., Nomura, N., & Shimada, I. (2007). Structural basis of the collagen-binding mode of discoidin domain receptor 2. EMBO Journal, 26(18), 4168-4176. https://doi.org/10.1038/sj.emboj.7601833