Enzyme-linked receptor

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==Activin receptor==
==Activin receptor==
*[[Activin receptor]]
*[[Activin receptor]]
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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.
==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'']]

Revision as of 11:10, 10 May 2021

Glycosylated mouse toll-like receptor 3 dimer complex with double-stranded RNA 3ciy

Drag the structure with the mouse to rotate

References and Notes

  1. 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

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Alexander Berchansky

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