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Receptor protein serine/threonine kinase

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Receptor protein serine/threonine kinase
Identifiers
EC no.2.7.11.30
CAS no.146702-86-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

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.{{cite journal}}: CS1 maint: unflagged free DOI (link)