Ontology highlight
ABSTRACT:
SUBMITTER: Kato M
PROVIDER: S-EPMC1142596 | biostudies-literature | 2005 May
REPOSITORIES: biostudies-literature
Kato Masato M Chuang Jacinta L JL Tso Shih-Chia SC Wynn R Max RM Chuang David T DT
The EMBO journal 20050428 10
The human pyruvate dehydrogenase complex (PDC) is regulated by reversible phosphorylation by four isoforms of pyruvate dehydrogenase kinase (PDK). PDKs phosphorylate serine residues in the dehydrogenase (E1p) component of PDC, but their amino-acid sequences are unrelated to eukaryotic Ser/Thr/Tyr protein kinases. PDK3 binds to the inner lipoyl domains (L2) from the 60-meric transacetylase (E2p) core of PDC, with concomitant stimulated kinase activity. Here, we present crystal structures of the P ...[more]