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

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

doi:10.1107/S0907444907009110

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

Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):587-96. doi: 10.1107/S0907444907009110. Epub 2007 Apr 21.

Authors

Philip Day¹, Andrew Sharff, Lina Parra, Anne Cleasby, Mark Williams, Stefan Hörer, Herbert Nar, Norbert Redemann, Ian Tickle, Jeff Yon

Affiliation

¹ Astex Therapeutics Ltd, 436 Cambridge Science Park, Milton Road, Cambridge CB4 0QA, England. [email protected]

PMID: 17452784
DOI: 10.1107/S0907444907009110

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.

MeSH terms

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

Substances

Ribonucleotides
Aminoimidazole Carboxamide
Adenosine Monophosphate
Adenylate Kinase
AICA ribonucleotide