2v8q
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(New page: 200px<br /> <applet load="2v8q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v8q, resolution 2.10Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 21:01, 29 October 2007
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CRYSTAL STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN AMPK IN COMPLEXES WITH AMP
Overview
AMP-activated protein kinase (AMPK) regulates cellular metabolism in, response to the availability of energy and is therefore a target for type, II diabetes treatment. It senses changes in the ratio of AMP/ATP by, binding both species in a competitive manner. Thus, increases in the, concentration of AMP activate AMPK resulting in the phosphorylation and, differential regulation of a series of downstream targets that control, anabolic and catabolic pathways. We report here the crystal structure of, the regulatory fragment of mammalian AMPK in complexes with AMP and ATP., The phosphate groups of AMP/ATP lie in a groove on the surface of the, gamma domain, which is lined with basic residues, many of which are, associated with disease-causing mutations. Structural and solution studies, reveal ... [(full description)]
About this Structure
2V8Q is a [Protein complex] structure of sequences from [Homo sapiens] and [Rattus norvegicus] with AMP as [ligand]. Active as [[1]], with EC number [2.7.11.1]. Full crystallographic information is available from [OCA].
Reference
Structural basis for AMP binding to mammalian AMP-activated protein kinase., Xiao B, Heath R, Saiu P, Leiper FC, Leone P, Jing C, Walker PA, Haire L, Eccleston JF, Davis CT, Martin SR, Carling D, Gamblin SJ, Nature. 2007 Sep 12;. PMID:17851531
Page seeded by OCA on Mon Oct 29 23:05:45 2007
Categories: Homo sapiens | Protein complex | Rattus norvegicus | Carling, D. | Davis, C.T. | Eccleston, J.F. | Gamblin, S.J. | Haire, L. | Heath, R. | Jing, C. | Leiper, F.C. | Leone, P. | Martin, S.R. | Saiu, P. | Walker, P.A. | Xiao, B. | AMP | Cbs domain | Kinase | Magnesium | Nucleotide-binding | Phosphorylation | Serine/threonine-protein kinase | Transferase