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: 2022-03-16)

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

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: 17703188
DOI: 10.1038/sj.emboj.7601833

Experimental method

SOLUTION NMR