腺苷酸活化蛋白激酶发生核苷酸依赖的构象变化。
AMP-activated protein kinase undergoes nucleotide-dependent conformational changes.
机构信息
MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.
出版信息
Nat Struct Mol Biol. 2012 Jun 3;19(7):716-8. doi: 10.1038/nsmb.2319.
The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the γ subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the γ subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation.
能量传感器 AMP 激活的蛋白激酶（AMPK）是一种异三聚体复合物，通过 AMP 结合到 γ 亚基上变构激活。哺乳动物 AMPK 核心的晶体结构揭示了在存在 ATP 的情况下，γ 亚基的核苷酸结合位点 3 被封闭。然而，在 AMP 的存在下，该位点被占据。突变研究表明，位点 3 和 4 对于 AMPK 的变构激活很重要。
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