FGG
Gene Ontology Biological Process
- blood coagulation [TAS]
- cell-matrix adhesion [IDA]
- cellular protein complex assembly [IDA]
- extracellular matrix organization [TAS]
- negative regulation of endothelial cell apoptotic process [IDA]
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [IDA]
- platelet activation [TAS]
- platelet aggregation [IDA]
- platelet degranulation [TAS]
- positive regulation of ERK1 and ERK2 cascade [IDA]
- positive regulation of exocytosis [IDA]
- positive regulation of heterotypic cell-cell adhesion [IDA]
- positive regulation of peptide hormone secretion [IDA]
- positive regulation of protein secretion [IDA]
- positive regulation of substrate adhesion-dependent cell spreading [NAS]
- positive regulation of vasoconstriction [IDA]
- protein polymerization [IMP]
- response to calcium ion [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
FGG
Gene Ontology Biological Process
- blood coagulation [TAS]
- cell-matrix adhesion [IDA]
- cellular protein complex assembly [IDA]
- extracellular matrix organization [TAS]
- negative regulation of endothelial cell apoptotic process [IDA]
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [IDA]
- platelet activation [TAS]
- platelet aggregation [IDA]
- platelet degranulation [TAS]
- positive regulation of ERK1 and ERK2 cascade [IDA]
- positive regulation of exocytosis [IDA]
- positive regulation of heterotypic cell-cell adhesion [IDA]
- positive regulation of peptide hormone secretion [IDA]
- positive regulation of protein secretion [IDA]
- positive regulation of substrate adhesion-dependent cell spreading [NAS]
- positive regulation of vasoconstriction [IDA]
- protein polymerization [IMP]
- response to calcium ion [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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 crystal structure of fragment double-D from cross-linked lamprey fibrin reveals isopeptide linkages across an unexpected D-D interface.
The crystal structure of fragment double-D from factor XIII-cross-linked lamprey fibrin has been determined at 2.9 A resolution. The 180 kDa covalent dimer was cocrystallized with the peptide Gly-His-Arg-Pro-amide, which in many fibrinogens, but not that of lamprey, corresponds to the B-knob exposed by thrombin. The structure was determined by molecular replacement, a recently determined structure of lamprey fragment D ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FGG FGG | Co-crystal Structure 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. | Low | - | BioGRID | - |
Curated By
- BioGRID