Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP.

Day, Philip; Sharff, Andrew; Parra, Lina; Cleasby, Anne; Williams, Mark; Hörer, Stefan; Nar, Herbert; Redemann, Norbert; Tickle, Ian; Yon, Jeff

Day, Philip; Sharff, Andrew; Parra, Lina; Cleasby, Anne; Williams, Mark; Hörer, Stefan; Nar, Herbert; Redemann, Norbert; Tickle, Ian; Yon, Jeff.

Affiliation

Day P; Astex Therapeutics Ltd, 436 Cambridge Science Park, Milton Road, Cambridge CB4 0QA, England. p.day@astex-therapeutics.com

Acta Crystallogr D Biol Crystallogr ; 63(Pt 5): 587-96, 2007 May.

Article in En | MEDLINE | ID: mdl-17452784

ABSTRACT

AMP-activated kinase (AMPK) is central to sensing energy status in eukaryotic cells via binding of AMP and ATP to CBS (cystathionine beta-synthase) domains in the regulatory gamma subunit. The structure of a CBS-domain pair from human AMPK gamma1 in complex with the physiological activator AMP and the pharmacological activator ZMP (AICAR) is presented.

Subject(s)

Adenosine Monophosphate/chemistry; Adenylate Kinase/chemistry; Aminoimidazole Carboxamide/analogs & derivatives; Ribonucleotides/chemistry; Amino Acid Sequence; Aminoimidazole Carboxamide/chemistry; Crystallization; Crystallography, X-Ray; Humans; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid

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Collection: 01-internacional Database: MEDLINE Main subject: Ribonucleotides / Adenosine Monophosphate / Adenylate Kinase / Aminoimidazole Carboxamide Limits: Humans Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 2007 Type: Article Affiliation country: United kingdom

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