FST
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
BMPR2
Gene Ontology Biological Process
- BMP signaling pathway [IDA, IMP, ISS, TAS]
- activin receptor signaling pathway [TAS]
- anterior/posterior pattern specification [ISS]
- artery development [ISS]
- blood vessel remodeling [ISS]
- cellular response to starvation [IEP]
- chondrocyte development [IMP]
- lung alveolus development [ISS]
- lymphangiogenesis [ISS]
- lymphatic endothelial cell differentiation [ISS]
- mesoderm formation [ISS]
- negative regulation of DNA biosynthetic process [IMP]
- negative regulation of cell growth [IDA]
- negative regulation of chondrocyte proliferation [IMP]
- negative regulation of systemic arterial blood pressure [IMP]
- negative regulation of vasoconstriction [ISS]
- positive regulation of BMP signaling pathway [IMP]
- positive regulation of bone mineralization [IMP]
- positive regulation of endothelial cell migration [IMP]
- positive regulation of endothelial cell proliferation [IMP]
- positive regulation of epithelial cell migration [IDA]
- positive regulation of osteoblast differentiation [IMP]
- positive regulation of pathway-restricted SMAD protein phosphorylation [IMP]
- regulation of cell proliferation [IMP]
- regulation of lung blood pressure [IMP, ISS]
- retina vasculature development in camera-type eye [ISS]
- transcription from RNA polymerase II promoter [IMP]
- transmembrane receptor protein serine/threonine kinase signaling pathway [IDA]
- vascular endothelial growth factor receptor signaling pathway [ISS]
- venous blood vessel development [ISS]
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 structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding.
TGF-beta ligands stimulate diverse cellular differentiation and growth responses by signaling through type I and II receptors. Ligand antagonists, such as follistatin, block signaling and are essential regulators of physiological responses. Here we report the structure of activin A, a TGF-beta ligand, bound to the high-affinity antagonist follistatin. Two follistatin molecules encircle activin, neutralizing the ligand by burying one-third of ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID