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

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.

SUBMITTER: Ichikawa O

PROVIDER: S-EPMC2230669 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature

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

Ichikawa Osamu O Osawa Masanori M Nishida Noritaka N Goshima Naoki N Nomura Nobuo N Shimada Ichio I

The EMBO journal 20070816 18

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, cons ...[more]

PMID: 17703188

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