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2FIB

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

Summary for 2FIB
Entry DOI10.2210/pdb2fib/pdb
DescriptorFIBRINOGEN, GLY-PRO-ARG-PRO, CALCIUM ION, ... (4 entities in total)
Functional Keywordsfibrinogen, blood coagulation, fibrin polymerization, complex (blood coagulation-peptide), complex (blood coagulation-peptide) complex, complex (blood coagulation/peptide)
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P02679
Total number of polymer chains2
Total formula weight30709.99
Authors
Pratt, K.P.,Cote, H.C.F.,Chung, D.W.,Stenkamp, R.E.,Davie, E.W. (deposition date: 1997-06-03, release date: 1997-10-15, Last modification date: 2024-10-16)
Primary citationPratt, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

237735

数据于2025-06-18公开中

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