1FBR

FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR

1FBR の概要

• エントリーDOI: 10.2210/pdb1fbr/pdb
• 分子名称: FIBRONECTIN (1 entity in total)
• 機能のキーワード: cell adhesion 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: 10534.70

構造登録者

Phan, I.Q.H.,Williams, M.J.,Campbell, I.D. (登録日: 1995-08-08, 公開日: 1995-10-15, 最終更新日: 2024-11-13)

主引用文献

Williams, M.J.,Phan, I.,Harvey, T.S.,Rostagno, A.,Gold, L.I.,Campbell, I.D.
Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity.
J.Mol.Biol., 235:1302-1311, 1994

PubMed Abstract: The tertiary structure of the fourth and fifth type 1 module pair from the N terminus of human fibronectin, has been determined by two-dimensional homonuclear 1H nuclear magnetic resonance (NMR) spectroscopy. Comparison of each module fold with those of two other type 1 modules shows that the type 1 "consensus" structure is conserved in the pair. The modules connect end-to-end to form an elongated structure with a limited clockwise twist around the long axis, from N to C terminus. The short five residue linker sequence forms a tight loop and the relative orientation of the two modules is maintained by fixed and intimate hydrophobic contacts, dominated by a non-conserved tryptophan residue from the fourth type 1 module. The protein binds specifically to fibrin in an ELISA and surface accessible residues that may be involved in this and other protein interactions can be identified. The structure provides an insight into how chains of type 1 modules may link up in intact fibronectin.

PubMed: 8308892
DOI: 10.1006/jmbi.1994.1083

実験手法

SOLUTION NMR