2CG6

Second and third fibronectin type I module pair (crystal form I).

2CG6 の概要

• エントリーDOI: 10.2210/pdb2cg6/pdb
• 関連するPDBエントリー: 1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2FN2 2FNB
• 分子名称: HUMAN FIBRONECTIN, SULFATE ION (3 entities in total)
• 機能のキーワード: cell adhesion, glycoprotein, heparin-binding, signaling protein, acute phase, alternative splicing, phosphorylation, pyrrolidone carboxylic acid, sulfation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P02751
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10216.45

構造登録者

Rudino-Pinera, E.,Ravelli, R.B.G.,Sheldrick, G.M.,Nanao, M.H.,Werner, J.M.,Schwarz-Linek, U.,Potts, J.R.,Garman, E.F. (登録日: 2006-02-27, 公開日: 2007-02-27, 最終更新日: 2017-08-30)

主引用文献

Rudino-Pinera, E.,Ravelli, R.B.G.,Sheldrick, G.M.,Nanao, M.H.,Korostelev, V.V.,Werner, J.M.,Schwarz-Linek, U.,Potts, J.R.,Garman, E.F.
The Solution and Crystal Structures of a Module Pair from the Staphylococcus Aureus-Binding Site of Human Fibronectin-A Tale with a Twist.
J.Mol.Biol., 368:833-, 2007

PubMed Abstract: An important goal of structural studies of modular proteins is to determine the inter-module orientation, which often influences biological function. The N-terminal domain of human fibronectin (Fn) is composed of a string of five type 1 modules (F1). Despite their small size, to date F1 modules have proved intractable to X-ray structure solution, although there are several NMR structures available. Here, we present the first structures (two X-ray models and an NMR-derived model) of the (2)F1(3)F1 module pair, which forms part of the binding site for Fn-binding proteins from pathogenic bacteria. The crystallographic structure determination was aided by the novel technique of UV radiation damage-induced phasing. The individual module structures are very similar in all three models. In the NMR structure and one of the X-ray structures, a similar but smaller interdomain interface than that observed previously for (4)F1(5)F1 is seen. The other X-ray structure has a different interdomain orientation. This work underlines the benefits of combining X-ray and NMR data in the studies of multi-domain proteins.

PubMed: 17368672
DOI: 10.1016/J.JMB.2007.02.061

実験手法

X-RAY DIFFRACTION (1.55 Å)