2FIB

RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) COMPLEXED TO THE PEPTIDE GLY-PRO-ARG-PRO AT PH 6.0

2FIB の概要

• エントリーDOI: 10.2210/pdb2fib/pdb
• 分子名称: FIBRINOGEN, GLY-PRO-ARG-PRO, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: fibrinogen, blood coagulation, fibrin polymerization, complex (blood coagulation-peptide), complex (blood coagulation-peptide) complex, complex (blood coagulation/peptide)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02679
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30709.99

構造登録者

Pratt, K.P.,Cote, H.C.F.,Chung, D.W.,Stenkamp, R.E.,Davie, E.W. (登録日: 1997-06-03, 公開日: 1997-10-15, 最終更新日: 2024-10-16)

主引用文献

Pratt, K.P.,Cote, H.C.,Chung, D.W.,Stenkamp, R.E.,Davie, E.W.
The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro.
Proc.Natl.Acad.Sci.USA, 94:7176-7181, 1997

PubMed Abstract: After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the newly exposed N-terminal Gly-Pro-Arg sequence of the alpha chain of one fibrin molecule and the C-terminal region of a gamma chain of an adjacent fibrin(ogen) molecule. In this report, the polymerization pocket has been identified by determining the crystal structure of a 30-kDa C-terminal fragment of the fibrin(ogen) gamma chain complexed with the peptide Gly-Pro-Arg-Pro. This peptide mimics the N terminus of the alpha chain of fibrin. The conformational change in the protein upon binding the peptide is subtle, with electrostatic interactions primarily mediating the association. This is consistent with biophysical experiments carried out over the last 50 years on this fundamental polymerization reaction.

PubMed: 9207064
DOI: 10.1073/pnas.94.14.7176

実験手法

X-RAY DIFFRACTION (2.01 Å)