AMP-activated protein kinase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='4rer' size='450' side='right' scene='49/493732/Cv/1' caption='Human AMP-activated protein kinase α1 subunit ( | + | <StructureSection load='4rer' size='450' side='right' scene='49/493732/Cv/1' caption='Human AMP-activated protein kinase α1 subunit (deeppink) +β2 subunit (green) +γ1 subunit (cyan) complex with AMP, staurosporine, cyclodextrin and HEPES (PDB code [[4rer]])'> |
== Function == | == Function == | ||
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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/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. |
</StructureSection> | </StructureSection> | ||
Revision as of 09:07, 12 November 2015
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3D structures of AMP-activated protein kinase
Updated on 12-November-2015
