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  • Title: Structural basis of the collagen-binding mode of discoidin domain receptor 2.
    Author: Ichikawa O, Osawa M, Nishida N, Goshima N, Nomura N, Shimada I.
    Journal: EMBO J; 2007 Sep 19; 26(18):4168-76. PubMed ID: 17703188.
    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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