Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP.
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.
Day
Philip
P
Astex Therapeutics Ltd, 436 Cambridge Science Park, Milton Road, Cambridge CB4 0QA, England. p.day@astex-therapeutics.com
Sharff
Andrew
A
Parra
Lina
L
Cleasby
Anne
A
Williams
Mark
M
Hörer
Stefan
S
Nar
Herbert
H
Redemann
Norbert
N
Tickle
Ian
I
Yon
Jeff
J
D000249:Adenosine Monophosphate / Q000737:chemistry*; D000263:Adenylate Kinase / Q000737:chemistry*; D000595:Amino Acid Sequence; D000620:Aminoimidazole Carboxamide / Q000031:analogs & derivatives* / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012265:Ribonucleotides / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D012265:Ribonucleotides; D000620:Aminoimidazole Carboxamide; D000249:Adenosine Monophosphate; D000263:Adenylate Kinase; C031143:AICA ribonucleotide