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

Acta crystallographica. Section D, Biological crystallography ·Vol. 63 ·No. Pt 5 ·2007-05-00 ·Pages 587-96

Day P, Sharff A, Parra L, Cleasby A, Williams M, Hörer S, Nar H, Redemann N, Tickle I, Yon J

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,chemistry Crystallization Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Conformation Ribonucleotides/chemistry Sequence Homology, Amino Acid

Chemicals

Ribonucleotides Aminoimidazole Carboxamide Adenosine Monophosphate Adenylate Kinase AICA ribonucleotide

Authors & Affiliations

10 authors, click to expand affiliations / ORCID

Day Philip

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

Sharff Andrew

Parra Lina

Cleasby Anne

Williams Mark

Hörer Stefan

Nar Herbert

Redemann Norbert

Tickle Ian

Yon Jeff

Article Info

Journal

Acta crystallographica. Section D, Biological crystallography

Abbr.

Acta Crystallogr D Biol Crystallogr

ISSN

0907-4449

DOI

10.1107/S0907444907009110

p.day@astex-therapeutics.com

Published

2007-05-00

Epub

2007-00-21

Pages

587-96

Language

English

Region

United States

NLM ID

9305878

Subset

External Links

PubMed source DOI: 10.1107/S0907444907009110 View journal details

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

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