AMP-activated protein kinase
From Proteopedia
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| - | + | <StructureSection load='4rer' size='450' side='right' scene='' caption='Human AMP-activated protein kinase α1 subunit (grey) +β2 subunit (green) +γ1 subunit (gold) complex with AMP, staurosporine, cyclodextrin and HEPES (PDB code [[4rer]])'> | |
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== Function == | == Function == | ||
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AMPK is a heterotrimer: <br /> '''AMPK α subunit''' is the catalytic subunit and contains Thr174 (TPO) or Ser108 (SEP) which undergoes phosphorylation. <br /> '''AMPK β subunit''' is a scaffold on which the heterotrimer assembles. <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 /> '''AMPK α subunit''' is the catalytic subunit and contains Thr174 (TPO) or Ser108 (SEP) which undergoes phosphorylation. <br /> '''AMPK β subunit''' is a scaffold on which the heterotrimer assembles. <br /> '''AMPK γ subunit''' detects shifts in AMP:ATP ratio via its 4 cystathionine β synthase (CBS) domains. The active site binds AMP. | ||
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| + | </StructureSection> | ||
==3D structures of AMP-activated protein kinase== | ==3D structures of AMP-activated protein kinase== | ||
Revision as of 08:35, 12 November 2015
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3D structures of AMP-activated protein kinase
Updated on 12-November-2015
