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Molecular Biology Reagents> | Te kinase domain of human BMPR2 (residues 189–517) was subcloned into the pNIC-CH vector and transformed into E. coli strain BL21(DE3)R3-pRARE2 for expression. Cultures were induced with 1mM IPTG overnight at 18 °C and the cells harvested and lysed by ultrasonication. Recombinant BMPR2 protein was recovered from the lysate by capture on Ni-IDA resin (Genscript) bufered in 50mM HEPES pH 7.5, 500mM NaCl, 5% glycerol, 5mM imidazole, 0.5mM TCEP. | Get A Quote |
Bone morphogenetic proteins (BMPs) are secreted ligands of the transforming growth factor-β (TGF-β) family that control embryonic patterning, as well as tissue development and homeostasis. Loss of function mutations in the type II BMP receptor BMPR2 are the leading cause of pulmonary arterial hypertension (PAH), a rare disease of vascular occlusion that leads to high blood pressure in the pulmonary arteries. To understand the structural consequences of these mutations, we determined the crystal structure of the human wild-type BMPR2 kinase domain at 2.35 Å resolution. The structure revealed an active conformation of the catalytic domain that formed canonical interactions with the bound ligand Mg-ADP. Disea... More