Activin receptor
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | 3D structure of the kinase domain of Acvr1 complex with inhibitor shows <scene name='84/843934/Cv/3'>the inhibitor forming various interactions</scene> with the protein including a <scene name='84/843934/Cv/5'>hydrogen bonds to His residues</scene> and a <scene name='84/843934/Cv/6'>water bridged hydrogen bond to the catalytic lysine</scene><ref>PMID:25101911</ref>. | + | 3D structure of the kinase domain of Acvr1 complex with inhibitor shows <scene name='84/843934/Cv/3'>the inhibitor forming various interactions</scene> with the protein including a <scene name='84/843934/Cv/5'>hydrogen bonds to His residues</scene> and a <scene name='84/843934/Cv/6'>water bridged hydrogen bond to the catalytic lysine</scene><ref>PMID:25101911</ref>. Water molecule is shown as red sphere. |
</StructureSection> | </StructureSection> | ||
Revision as of 16:03, 6 May 2020
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3D structures of activin receptor
Updated on 06-May-2020
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
