BMPR2

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Bone morphogenetic protein receptor type II
Genetic data
Gene code:	HUGO code:BMPR2
Protein Structure/Function
Protein type:	Receptor serine/threonine kinase
Functions:	Receptor for TGF beta ligands - BMP's
Domains:	TM domain, S/T kinase
Other
Taxa expressing:	Homo sapiens; homologs: many metazoan phyla
Cell types:	many; expressed highly in heart and liver
Subcellular localization:	Plasma membrane
Enzymatic Data
Catalytic activity:	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate
Cofactor(s):	Magnesium or manganese
Medical/Biotechnological data
Diseases:	Primary pulmonary hypertension (PPH1) Mendelian Inheritance in Man (OMIM) 178600

Bone morphogenetic protein receptor type II or BMPR2 is a serine/threonine receptor kinase. It binds Bone morphogenetic proteins, members of the TGF beta superfamily of ligands. BMPs are involved in host of cellular functions including osteogenesis, cell growth and cell differentiation. Signaling in the BMP pathway begins with the binding of a BMP to the the type II receptor. This causes the recruitment of a BMP type I receptor, which it phosphorylates. The Type I receptor phosphorylates an R-SMAD a transcriptional regulator.

Identifiers
Symbol	BMPR2
HUGO	1078
Entrez	659
OMIM	600799
RefSeq	NM_001204
UniProt	Q13873
Other data
Locus	Chr. 2 q33

[edit] Function

Unlike the TGFβ type II receptor, which has a high affinity for TGF-β1, BMPR2 does not have a high affinity for BMP-2, BMP-7 and BMP-4, unless it is co-expressed with a type I BMP receptor^[1]. In TGF beta signaling all of the receptors exist in homodimers before ligand binding. In the case of BMP receptors only a small fraction of the receptors exist in homomeric forms before ligand binding. Once a ligand has bound to a receptor, the amount of homomeric receptor oligomers increase, suggesting that the equilibrium shifts towards the homodimeric form^[1]. The low affinity for ligands suggests that BMPR2 may differ in the from other type II TGF beta receptors in that the ligand may bind the type I receptor first^[2].

[edit] References

1. ^ ^{a b} Gilboa, L; Nohe A, Geissendorfer T, Sebald W, Henis YI, Knaus P. (Mar 2000). "Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors". Mol Biol Cell. 11 (3). Retrieved on 2006-07-03. 
2. ^ Kirsch, T; Nickel J, Sebald W. (Jul 2000). "BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II". EMBO J. 19 (13). PubMed. Retrieved on 2006-07-03.