AMP-activated protein kinase

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== Structural highlights ==
== Structural highlights ==
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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. There are 2 β subunits. β subunit contains <scene name='49/493732/Cv/7'>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/9'>The active site binds 3 AMPs</scene>.
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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. There are 2 β subunits. β subunit contains <scene name='49/493732/Cv/7'>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/9'>The active site binds 3 AMPs</scene>.<ref>PMID:25412657</ref>
</StructureSection>
</StructureSection>
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}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:44, 12 November 2015

Human AMP-activated protein kinase α1 subunit (deeppink) +β2 subunit (green) +γ1 subunit (cyan) complex with AMP, staurosporine, cyclodextrin and HEPES (PDB code 4rer)

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3D structures of AMP-activated protein kinase

Updated on 12-November-2015

References

  1. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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