2bu5
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CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS
OverviewOverview
Pyruvate dehydrogenase kinase (PDHK) regulates the activity of the, pyruvate dehydrogenase multienzyme complex. PDHK inhibition provides a, route for therapeutic intervention in diabetes and cardiovascular, disorders. We report crystal structures of human PDHK isozyme 2 complexed, with physiological and synthetic ligands. Several of the PDHK2 structures, disclosed have C-terminal cross arms that span a large trough region, between the N-terminal regulatory (R) domains of the PDHK2 dimers. The, structures containing bound ATP and ADP demonstrate variation in the, conformation of the active site lid, residues 316-321, which enclose the, nucleotide beta and gamma phosphates at the active site in the C-terminal, catalytic domain. We have identified three novel ligand binding sites, located in ... [(full description)]
About this StructureAbout this Structure
2BU5 is a [Single protein] structure of sequence from [Homo sapiens] with TF1 as [ligand]. Active as [[1]], with EC number [2.7.1.99]. Full crystallographic information is available from [OCA].
ReferenceReference
Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands., Knoechel TR, Tucker AD, Robinson CM, Phillips C, Taylor W, Bungay PJ, Kasten SA, Roche TE, Brown DG, Biochemistry. 2006 Jan 17;45(2):402-15. PMID:16401071
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