AMP-activated protein kinase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | AMPK is a heterotrimer: <br /> <scene name='49/493732/Cv/ | + | AMPK is a heterotrimer: <br /> <scene name='49/493732/Cv/10'>AMPK α subunit</scene> is the catalytic subunit and contains <scene name='49/493732/Cv/11'>Thr174 (TPO) which undergoes phosphorylation</scene>. <br /> <scene name='49/493732/Cv/5'>AMPK β subunit</scene> is a scaffold on which the heterotrimer assembles. There are 2 β subunits. β subunit contains <scene name='49/493732/Cv/12'>phosphorylated Ser108 (SEP)</scene>. <br /> <scene name='49/493732/Cv/8'>AMPK γ subunit</scene> detects shifts in AMP:ATP ratio via its 4 cystathionine β synthase (CBS) domains. <scene name='49/493732/Cv/13'>The active site binds 3 AMPs</scene>.<ref>PMID:25412657</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 13:27, 7 May 2018
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3D structures of AMP-activated protein kinase
Updated on 07-May-2018
References
- ↑ Li X, Wang L, Zhou XE, Ke J, de Waal PW, Gu X, Tan MH, Wang D, Wu D, Xu HE, Melcher K. Structural basis of AMPK regulation by adenine nucleotides and glycogen. Cell Res. 2014 Nov 21. doi: 10.1038/cr.2014.150. PMID:25412657 doi:http://dx.doi.org/10.1038/cr.2014.150
