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

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

研究成果: Article査読

89 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)4168-4176
ページ数9
ジャーナルEMBO Journal
26
18
DOI
出版ステータスPublished - 2007 9月 19
外部発表はい

ASJC Scopus subject areas

  • 神経科学一般
  • 分子生物学
  • 生化学、遺伝学、分子生物学一般
  • 免疫学および微生物学一般

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