AMP-activated protein kinase

From Proteopedia

Revision as of 10:01, 7 March 2013

Template:STRUCTURE 2v8q AMP-activated protein kinase (AMPK) is a nuclear receptor which regulates cellular uptake of glucose, β-oxidation of fatty acids and biogenesis of glucose transporter thus playing a role in cellular energy homeostasis by phosphorylating key proteins. In response to low levels of ATP, AMPK activates energy-producing pathways and inhibits energy-consuming pathways. AMPK is a heterotrimer. AMPK γ subunit detects shifts in AMP:ATP ratio via its 4 cystathionine β synthase (CBS) domains. AMPK α subunit is the catalytic subunit and contains Thr172 (TPO) which undergoes phosphorylation. AMPK β subunit is a scaffold on which the heterotrimer assembles.

3D structures of AMP-activated protein kinase

Updated on 07-March-2013

AMPK α subunit

2h6d - hAMPK α2 subunit – human
2yza - hAMPK α2 subunit (mutant)
3aqv - hAMPK α2 subunit (mutant) + inhibitor

AMPK β subunit

1z0m, 1z0n – rAMPK β1 subunit – rat
2f15 - hAMPK β2 subunit

AMPK γ subunit

2uv4, 2uv5 - hAMPK γ1 subunit CBS 3+4 domains + AMP
2uv6, 2uv7 - hAMPK γ1 subunit CBS 3+4 domains (mutant) + AMP

AMPK α+β+γ subunits

2y94 - rAMPK α1,β2,γ1 subunits + TPO + AMP
2v8q - rAMPK α1,β2,γ1 subunits + AMP
2v92, 2v9j - rAMPK α1,β2,γ1 subunits + ATP + AMP
2y8l, 2y8q - rAMPK α1,β2,γ1 subunits + ADP
2ya3 - rAMPK α1,β2,γ1 subunits + coumarin-ADP + AMP