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spinqualitylabelsall models Human Acvr1 kinase domain complex with inhibitor, ethylene glycol and citrate (PDB code 4bgg) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Activin receptors (Acvr) are integral to the activin and myostatin signalling pathway. Binding of activin to the Acvr on muscle cell membrane leads to enhanced muscle protein breakdown and debilitating loss of muscle mass and functional capacity[1]. Disease A mutation in Acrv1 exists in individuals with the rare developmental disorder fibrodysplasia ossificans progressiva[2]. Relevance Increased activin/Acvr2 signalling links aging and heart failure pathobiology and that targeted inhibition of this catabolic pathway may form a therapeutic strategy for multiple forms of hear failure[3]. Structural highlights 3D structure of the kinase domain of Acvr1 complex with inhibitor shows with the protein including a and a [4]. Water molecule is shown as red sphere.

3D structures of activin receptor

Updated on 04-March-2021

References

1. ↑ Han HQ, Zhou X, Mitch WE, Goldberg AL. Myostatin/activin pathway antagonism: molecular basis and therapeutic potential. Int J Biochem Cell Biol. 2013 Oct;45(10):2333-47. doi:, 10.1016/j.biocel.2013.05.019. Epub 2013 May 28. PMID:23721881 doi:http://dx.doi.org/10.1016/j.biocel.2013.05.019
2. ↑ Williams E, Bullock AN. Structural basis for the potent and selective binding of LDN-212854 to the BMP receptor kinase ALK2. Bone. 2017 Sep 12. pii: S8756-3282(17)30340-X. doi: 10.1016/j.bone.2017.09.004. PMID:28918311 doi:http://dx.doi.org/10.1016/j.bone.2017.09.004
3. ↑ Roh JD, Hobson R, Chaudhari V, Quintero P, Yeri A, Benson M, Xiao C, Zlotoff D, Bezzerides V, Houstis N, Platt C, Damilano F, Lindman BR, Elmariah S, Biersmith M, Lee SJ, Seidman CE, Seidman JG, Gerszten RE, Lach-Trifilieff E, Glass DJ, Rosenzweig A. Activin type II receptor signaling in cardiac aging and heart failure. Sci Transl Med. 2019 Mar 6;11(482). pii: 11/482/eaau8680. doi:, 10.1126/scitranslmed.aau8680. PMID:30842316 doi:http://dx.doi.org/10.1126/scitranslmed.aau8680
4. ↑ Mohedas AH, Wang Y, Sanvitale CE, Canning P, Choi S, Xing X, Bullock AN, Cuny GD, Yu PB. Structure-activity relationship of 3,5-diaryl-2-aminopyridine ALK2 inhibitors reveals unaltered binding affinity for fibrodysplasia ossificans progressiva causing mutants. J Med Chem. 2014 Oct 9;57(19):7900-15. doi: 10.1021/jm501177w. Epub 2014 Sep 4. PMID:25101911 doi:http://dx.doi.org/10.1021/jm501177w