AMP-activated protein kinase
From Proteopedia
(Difference between revisions)
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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> | 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> | ||
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| + | ==3D structures of AMP-activated protein kinase== | ||
| + | [[AMP-activated protein kinase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
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**[[2yza]] - hAMPK α2 subunit (mutant) <br /> | **[[2yza]] - hAMPK α2 subunit (mutant) <br /> | ||
**[[3aqv]] - hAMPK α2 subunit (mutant) + inhibitor<br /> | **[[3aqv]] - hAMPK α2 subunit (mutant) + inhibitor<br /> | ||
| + | **[[6bx6]] – hAMPK kinase domain (mutant) + inhibitor<br /> | ||
*AMPK β-1 carbohydrate-binding domain | *AMPK β-1 carbohydrate-binding domain | ||
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*Phosphorylated AMPK α-1+β-1+γ-1 | *Phosphorylated AMPK α-1+β-1+γ-1 | ||
| + | **[[6c9f]] – hAMPK + activator<br /> | ||
| + | **[[6c9g]], [[6c9h]], [[6c9j]] – hAMPK (mutant) + activator<br /> | ||
**[[4qfg]] – rAMPK (mutant) + AMP + staurosporine <br /> | **[[4qfg]] – rAMPK (mutant) + AMP + staurosporine <br /> | ||
| - | **[[5ufu]] – rAMPK + AMP + ADP + staurosporine + activator<br /> | + | **[[5ufu]], [[6e4u]], [[6e4t]], [[6e4w]] – rAMPK + AMP + ADP + staurosporine + activator<br /> |
**[[4qfr]], [[4qfs]], [[5t5t]] – rAMPK (mutant) + AMP + ADP + staurosporine + activator<br /> | **[[4qfr]], [[4qfs]], [[5t5t]] – rAMPK (mutant) + AMP + ADP + staurosporine + activator<br /> | ||
**[[5kq5]] – rAMPK + AMP + ADP + staurosporine + activator<br /> | **[[5kq5]] – rAMPK + AMP + ADP + staurosporine + activator<br /> | ||
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*Phosphorylated AMPK α-2+β-1+γ-1 | *Phosphorylated AMPK α-2+β-1+γ-1 | ||
| - | **[[4cfe]], [[5iso]] | + | **[[4cfe]], [[5iso]], [[4cff]], [[6b12u]] – hAMPK + AMP + staurosporine + benzimidazole derivative<br /> |
| - | + | ||
**[[4zhx]], [[5ezv]] – hAMPK + AMP + staurosporine + furan-2-posphonic derivative<br /> | **[[4zhx]], [[5ezv]] – hAMPK + AMP + staurosporine + furan-2-posphonic derivative<br /> | ||
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| + | *Phosphorylated AMPK α-2+β-2+γ-1 | ||
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| + | **[[6b2e]] – hAMPK + AMP + staurosporine + activator<br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:40, 14 March 2019
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3D structures of AMP-activated protein kinase
Updated on 14-March-2019
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
