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

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

doi:10.1038/sj.emboj.7601833

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

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

School of Pharmaceutical Sciences

Research output: Contribution to journal › Article

83 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 language	English
Pages (from-to)	4168-4176
Number of pages	9
Journal	EMBO Journal
Volume	26
Issue number	18
DOIs	https://doi.org/10.1038/sj.emboj.7601833
Publication status	Published - 2007 Sep 19

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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)

Cite this

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

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10.1038/sj.emboj.7601833