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
FGB
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 [IDA]
- 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
2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site.
We report two crystal structures, each at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) in the absence and presence of peptide ligands. The bound ligands, Gly-Pro-Arg-Pro-amide and Gly-His-Arg-Pro-amide, mimic the interactions of the thrombin exposed polymerization sites, "A" and "B", respectively. This report is the first to describe the structure of fragment D in the ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| FGB FGG | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3724013 |
Curated By
- BioGRID