3MQL

Crystal structure of the fibronectin 6FnI1-2FnII7FnI fragment

3MQL の概要

• エントリーDOI: 10.2210/pdb3mql/pdb
• 関連するPDBエントリー: 1E88 1E8B 3EJH 3GXE
• 分子名称: Fibronectin 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• 機能のキーワード: cell adhesion, fibronectin, collagen, gbd, fn2, fn1
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25450.20

構造登録者

Erat, M.C.,Campbell, I.D.,Vakonakis, I. (登録日: 2010-04-28, 公開日: 2010-08-25, 最終更新日: 2024-10-30)

主引用文献

Erat, M.C.,Schwarz-Linek, U.,Pickford, A.R.,Farndale, R.W.,Campbell, I.D.,Vakonakis, I.
Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI
J.Biol.Chem., 285:33764-33770, 2010

PubMed Abstract: Collagen and fibronectin (FN) are two abundant and essential components of the vertebrate extracellular matrix; they interact directly with cellular receptors and affect cell adhesion and migration. Past studies identified a FN fragment comprising six modules, (6)FnI(1-2)FnII(7-9)FnI, and termed the gelatin binding domain (GBD) as responsible for collagen interaction. Recently, we showed that the GBD binds tightly to a specific site within type I collagen and determined the structure of domains (8-9)FnI in complex with a peptide from that site. Here, we present the crystallographic structure of domains (6)FnI(1-2)FnII(7)FnI, which form a compact, globular unit through interdomain interactions. Analysis of NMR titrations with single-stranded collagen peptides reveals a dominant collagen interaction surface on domains (2)FnII and (7)FnI; a similar surface appears involved in interactions with triple-helical peptides. Models of the complete GBD, based on the new structure and the (8-9)FnI·collagen complex show a continuous putative collagen binding surface. We explore the implications of this model using long collagen peptides and discuss our findings in the context of FN interactions with collagen fibrils.

PubMed: 20739283
DOI: 10.1074/jbc.M110.139394

実験手法

X-RAY DIFFRACTION (3.004 Å)