2Z4F
Solution structure of the Discoidin Domain of DDR2
Summary for 2Z4F
| Entry DOI | 10.2210/pdb2z4f/pdb |
| NMR Information | BMRB: 15315 |
| Descriptor | Discoidin domain-containing receptor 2 (1 entity in total) |
| Functional Keywords | beta barrel, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: Q16832 |
| Total number of polymer chains | 1 |
| Total formula weight | 19393.71 |
| Authors | Ichikawa, O.,Osawa, M.,Nishida, N.,Goshima, N.,Nomura, N.,Shimada, I. (deposition date: 2007-06-16, release date: 2007-09-04, Last modification date: 2024-11-20) |
| Primary citation | Ichikawa, O.,Osawa, M.,Nishida, N.,Goshima, N.,Nomura, N.,Shimada, I. Structural basis of the collagen-binding mode of discoidin domain receptor 2 Embo J., 26:4168-4176, 2007 Cited by PubMed 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. PubMed: 17703188DOI: 10.1038/sj.emboj.7601833 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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