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Article

Structural basis for compound C inhibition of the human AMP-activated protein kinase α2 subunit kinase domain.

Acta crystallographica. Section D, Biological crystallography - 1 May 2011

Handa Noriko, Takagi Tetsuo, Saijo Shinya, Kishishita Seiichiro, Takaya Daisuke, Toyama Mitsutoshi, Terada Takaho, Shirouzu Mikako, Suzuki Atsushi, Lee Suni, Yamauchi Toshimasa, Okada-Iwabu Miki, Iwabu Masato, Kadowaki Takashi, Minokoshi Yasuhiko, Yokoyama Shigeyuki

Abstract excerpt

AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor to maintain energy balance at both the cellular and the whole-body levels and is therefore a potential target for drug design against metabolic syndrome, obesity and type 2 diabetes. Here, the crystal structure of the phosphorylated-state mimic T172D mutant kinase domain from the human AMPK α2 subunit is reported in the...

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Identifiers

PMID: 21543851
DOI: 10.1107/S0907444911010201

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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