BAIT

F2

PT, RPRGL2, THPH1
coagulation factor II (thrombin)
GO Process (24)
GO Function (5)
GO Component (7)
Homo sapiens
PREY

FGA

Fib2
fibrinogen alpha chain
Homo sapiens

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

The interaction of thrombin with fibrinogen. A structural basis for its specificity.

Stubbs MT, Oschkinat H, Mayr I, Huber R, Angliker H, Stone SR, Bode W

The structure of the ternary complex of human alpha-thrombin with a covalently bound analogue of fibrinopeptide A and a C-terminal hirudin peptide has been determined by X-ray diffraction methods at 0.25 nm resolution. Fibrinopeptide A folds in a compact manner, bringing together hydrophobic residues that slot into the apolar binding site of human alpha-thrombin. Fibrinogen residue Phe8 occupies the aryl-binding ... [more]

Eur. J. Biochem. May. 15, 1992; 206(1);187-95 [Pubmed: 1587268]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
FGA F2
Co-localization
Co-localization

Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

High-BioGRID
1504708

Curated By

  • BioGRID