Enzyme-linked receptor
From Proteopedia
(Difference between revisions)
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3D structure of the kinase domain of Activin receptor1 (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. | 3D structure of the kinase domain of Activin receptor1 (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. | ||
==Receptor-like serine/threonine protein kinase== | ==Receptor-like serine/threonine protein kinase== | ||
- | *[[Journal:Acta Cryst F:S2053230X20010122|Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from ''Arabidopsis thaliana'']] | + | *[[Journal:Acta Cryst F:S2053230X20010122|Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from ''Arabidopsis thaliana'']]<ref>doi 10.1107/S2053230X20010122</ref> |
+ | <scene name='85/857139/Cv/10'>Overall structure of TMK3-LRR domain. 1st orientation</scene> | ||
+ | |||
+ | <scene name='85/857139/Cv/11'>Overall structure of TMK3-LRR domain. 2nd orientation</scene>. The LRRNT, LRRs (numbered as indicated) and the non-LRR region of TMK3-LRR are colored in green, whitesmoke and blue, respectively. The three disulfide bonds (Cys54-Cys61, Cys315-Cys323 and Cys353-Cys361) are depicted in yellow. “N” and “C” represent N- and C-terminus, respectively. | ||
==Bone morphogenetic protein receptors== | ==Bone morphogenetic protein receptors== | ||
*[[Student Projects for UMass Chemistry 423 Spring 2012-4|Bone Morphogenetic Protein 7 and receptor]] | *[[Student Projects for UMass Chemistry 423 Spring 2012-4|Bone Morphogenetic Protein 7 and receptor]] |
Revision as of 11:13, 10 May 2021
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References and Notes
- ↑ 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
- ↑ Chen H, Kong Y, Chen J, Li L, Li X, Yu F, Ming Z. Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana. Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):384-390. doi:, 10.1107/S2053230X20010122. Epub 2020 Jul 29. PMID:32744250 doi:http://dx.doi.org/10.1107/S2053230X20010122