Structural basis of the collagen-binding mode of discoidin domain receptor 2 |
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Authors: | Ichikawa Osamu Osawa Masanori Nishida Noritaka Goshima Naoki Nomura Nobuo Shimada Ichio |
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Affiliation: | Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan. |
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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 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. |
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Keywords: | collagen discoidin domain receptor NMR protein–protein interaction transferred cross-saturation |
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