AMP-activated protein kinase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | AMPK is a heterotrimer: <br /> <scene name='49/493732/Cv/4'>AMPK α subunit</scene> is the catalytic subunit and contains <scene name='49/493732/Cv/3'>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. β subunit contains Ser108 (SEP) <br /> '''AMPK γ subunit''' detects shifts in AMP:ATP ratio via its 4 cystathionine β synthase (CBS) domains. The active site binds AMP. | + | AMPK is a heterotrimer: <br /> <scene name='49/493732/Cv/4'>AMPK α subunit</scene> is the catalytic subunit and contains <scene name='49/493732/Cv/3'>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. β subunit contains <scene name='49/493732/Cv/7'>phosphorylated Ser108 (SEP)</scene>. <br /> '''AMPK γ subunit''' detects shifts in AMP:ATP ratio via its 4 cystathionine β synthase (CBS) domains. The active site binds AMP. |
</StructureSection> | </StructureSection> | ||
Revision as of 09:14, 12 November 2015
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3D structures of AMP-activated protein kinase
Updated on 12-November-2015
