Receptor protein serine/threonine kinase
Receptor protein serine/threonine kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.11.30 | ||||||||
CAS no. | 146702-86-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a receptor protein serine/threonine kinase (EC 2.7.11.30) is an enzyme that catalyzes the chemical reaction
- ATP + [receptor-protein] ADP + [receptor-protein] phosphate
Thus, the two substrates of this enzyme are ATP and receptor protein, whereas its two products are ADP and receptor protein phosphate.
This enzyme belongs to the family of transferases, to be specific those transferring phosphorus-containing groups protein-serine/threonine kinases. The systematic name of this enzyme class is ATP:[receptor-protein] phosphotransferase. Other names in common use include activin receptor kinase, receptor type I serine/threonine protein kinase, receptor type II serine/threonine protein kinase, STK13, TGF-beta kinase, and receptor serine/threonine protein kinase. This enzyme participates in 7 metabolic pathways: MAPK signaling pathway, cytokine-cytokine receptor interaction, TGF beta signaling pathway, adherens junction, colorectal cancer, pancreatic cancer, and chronic myeloid leukemia.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2GOO, 2H62, 2H64, 2HLQ, and 2HLR.
References
- Wrana JL, Attisano L, Wieser R, Ventura F, Massague J (1994). "Mechanism of activation of the TGF-beta receptor". Nature. 370 (6488): 341–7. doi:10.1038/370341a0. PMID 8047140.
- Massague J, Chen YG (2000). "Controlling TGF-beta signaling". Genes Dev. 14 (6): 627–44. PMID 10733523.
- Lechleider RJ; Hemmati, P; Larisch-Bloch, S; Ajmera, R; Roberts, AB; Lechleider, RJ (1997). "Characterization of functional domains within Smad4/DPC4". J. Biol. Chem. 272 (21): 13690–6. doi:10.1074/jbc.272.21.13690. PMID 9153220.
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