1A21

TISSUE FACTOR (TF) FROM RABBIT

1A21 の概要

• エントリーDOI: 10.2210/pdb1a21/pdb
• 分子名称: TISSUE FACTOR (2 entities in total)
• 機能のキーワード: blood coagulation factor, fviia activation, cytokine receptor superfamily, extracellular domain, glycoprotein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Membrane ; Single-pass type I membrane protein : P24055
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50212.10

構造登録者

Muller, Y.A.,De Vos, A.M. (登録日: 1998-01-14, 公開日: 1998-05-27, 最終更新日: 2024-10-09)

主引用文献

Muller, Y.A.,Kelley, R.F.,de Vos, A.M.
Hinge bending within the cytokine receptor superfamily revealed by the 2.4 A crystal structure of the extracellular domain of rabbit tissue factor.
Protein Sci., 7:1106-1115, 1998

PubMed Abstract: Tissue factor (TF), a member of the cytokine receptor superfamily, is the obligate cofactor of coagulation factor VIIa (FVIIa), and has a pivotal role in initiating the extrinsic pathway of blood coagulation through formation of the TF x FVIIa complex. The crystal structure of the extracellular portion of rabbit TF has been solved at 2.35 A resolution and refined to a crystallographic R-value of 19.1% (free R-value, 27.7%). Like the human homologue, the extracellular portion consists of two fibronectin type III domains connected by a short alpha-helical segment. Unexpectedly, the two molecules in the crystallographic asymmetric unit differ in their relative domain-domain orientation, revealing unsuspected hinge motion consisting of a rotation of about 12.7 degrees around an axis intersecting the linker segment at residue 106. Superposition of rabbit tissue factor with free and bound human tissue factor allows for the detection of an identical, albeit smaller, hinge motion in human TF induced upon binding of FVIIa. This raises the possibility that a very similar hinge axis may be present in other members of the cytokine receptor superfamily.

PubMed: 9605315

実験手法

X-RAY DIFFRACTION (2.35 Å)