2H41

Solution structure of the second type III domain of human Fibronectin: minimized average structure

2H41 の概要

• エントリーDOI: 10.2210/pdb2h41/pdb
• 関連するPDBエントリー: 2H45
• NMR情報: BMRB: 7127
• 分子名称: Fibronectin (1 entity in total)
• 機能のキーワード: beta sandwich, cell adhesion, structural protein
• 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: 10202.06

構造登録者

Vakonakis, I.,Campbell, I.D. (登録日: 2006-05-23, 公開日: 2007-04-10, 最終更新日: 2024-05-29)

主引用文献

Vakonakis, I.,Staunton, D.,Rooney, L.M.,Campbell, I.D.
Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis.
Embo J., 26:2575-2583, 2007

PubMed Abstract: The process by which fibronectin (FN), a soluble multidomain protein found in tissue fluids, forms insoluble fibrillar networks in the extracellular matrix is poorly understood. Cryptic sites found in FN type III domains have been hypothesized to function as nucleation points, thereby initiating fibrillogenesis. Exposure of these sites could occur upon tension-mediated mechanical rearrangement of type III domains. Here, we present the solution structures of the second type III domain of human FN ((2)FNIII), and that of an interaction complex between the first two type III domains ((1-2)FNIII). The two domains are connected through a long linker, flexible in solution. A weak but specific interdomain interaction maintains (1-2)FNIII in a closed conformation that associates weakly with the FN N-terminal 30 kDa fragment (FN30 kDa). Disruption of the interdomain interaction by amino-acid substitutions dramatically enhances association with FN30 kDa. Truncation analysis of (1-2)FNIII reveals that the interdomain linker is necessary for robust (1-2)FNIII-FN30 kDa interaction. We speculate on the importance of this interaction for FN function and present a possible mechanism by which tension could initiate fibrillogenesis.

PubMed: 17464288
DOI: 10.1038/sj.emboj.7601694

実験手法

SOLUTION NMR