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- W57181813 abstract "Pyruvate dehydrogenase kinase 2 (PDHK2) is a unique mitochondrial protein kinase that regulates the activity of pyruvate dehydrogenase multienzyme complex (PDC). PDHK2 is an integral component of PDC tightly bound to the inner lipoyl-bearing domains (L2) of dihydrolipoyl transacetylase component (E2). In this study, we used a combination of molecular modeling and site-directed mutagenesis in order to identify the amino acid residues essential for the interaction between PDHK2 and L2. Based on the results of site-directed mutagenesis it appears that a number of PDHK2 residues located in the R domain (P22, L23, F28, F31, F44, L45, and L160) and in so-called “cross arm” structure (K368, R372, and K391) are critical in determining the strength of the interaction between PDHK2 and L2. The residues of L2 essential for recognition by PDHK2 include L140, K173, I176, E179A, and to a lesser extent D164, D172, and A174. Importantly, certain PDHK2 residues interfacing with L2, i.e. K17, P22, F31, F44, R372, and K391, are critical for the maintenance of enhanced PDHK2 activity in E2-bound state. The latter strongly suggests that an increase in the overall kinase activity associated with docking of PDHK2 to the 60-meric E2 assembly is due, in part, to the activation of PDHK2 caused by its interaction with L2 domain(s). This study was supported by PHS grant GM51262." @default.
- W57181813 created "2016-06-24" @default.
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- W57181813 date "2007-04-01" @default.
- W57181813 modified "2023-09-25" @default.
- W57181813 title "Recognition of inner lipoyl bearing domain of dihydrolipoyl transacetylase by pyruvate dehydrogenase kinase 2" @default.
- W57181813 doi "https://doi.org/10.1096/fasebj.21.5.a643-d" @default.
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