1FYC

INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX, NMR, 1 STRUCTURE

Summary for 1FYC

• Entry DOI: 10.2210/pdb1fyc/pdb
• Descriptor: DIHYDROLIPOAMIDE ACETYLTRANSFERASE (E2P) (1 entity in total)
• Functional Keywords: transferase, acyltransferase dihydrolipoamide, subunit, unlipoylated
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: P10515
• Total number of polymer chains: 1
• Total formula weight: 11661.32

Authors

Howard, M.J.,Fuller, C.,Broadhurst, R.W.,Quinn, J.,Yeaman, S.J.,Perham, R.N. (deposition date: 1997-02-21, release date: 1997-09-04, Last modification date: 2024-05-01)

Primary citation

Howard, M.J.,Fuller, C.,Broadhurst, R.W.,Perham, R.N.,Tang, J.G.,Quinn, J.,Diamond, A.G.,Yeaman, S.J.
Three-dimensional structure of the major autoantigen in primary biliary cirrhosis.
Gastroenterology, 115:139-146, 1998

PubMed Abstract: Primary biliary cirrhosis (PBC) is a chronic cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients' serum. The major autoantigen, recognized by antibodies from > 95% of patients with PBC, has been identified as the E2 component (E2p) of the pyruvate dehydrogenase multienzyme complex. Immunodominant sites on E2p have been localized to the inner of the two lipoyl domains, where the essential cofactor lipoic acid is attached covalently. The aim of this study was to determine the three-dimensional structure of the inner lipoyl domain of human E2p.

PubMed: 9649469

Experimental method

SOLUTION NMR