2Z4F

Solution structure of the Discoidin Domain of DDR2

2Z4F の概要

• エントリーDOI: 10.2210/pdb2z4f/pdb
• NMR情報: BMRB: 15315
• 分子名称: Discoidin domain-containing receptor 2 (1 entity in total)
• 機能のキーワード: beta barrel, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: Q16832
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19393.71

構造登録者

Ichikawa, O.,Osawa, M.,Nishida, N.,Goshima, N.,Nomura, N.,Shimada, I. (登録日: 2007-06-16, 公開日: 2007-09-04, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

SOLUTION NMR