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
Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.
In blood coagulation, units of the protein fibrinogen pack together to form a fibrin clot, but a crystal structure for fibrinogen is needed to understand how this is achieved. The structure of a core fragment (fragment D) from human fibrinogen has now been determined to 2.9 A resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous ... [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