1fyc
From Proteopedia
(New page: 200px<br /> <applet load="1fyc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fyc" /> '''INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEH...) |
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'''INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX, NMR, 1 STRUCTURE'''<br /> | '''INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX, NMR, 1 STRUCTURE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http:// | + | 1FYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: unlipoylated]] | [[Category: unlipoylated]] | ||
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Revision as of 13:49, 15 February 2008
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INNER LIPOYL DOMAIN FROM HUMAN PYRUVATE DEHYDROGENASE (PDH) COMPLEX, NMR, 1 STRUCTURE
Overview
BACKGROUND & AIMS: 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., METHODS: The domain was expressed in Escherichia coli; after purification, its structure was analyzed using nuclear magnetic resonance spectroscopy., RESULTS: The structure of the lipoyl domain from human E2p was determined, and the implications of the structure for autoimmune recognition were, assessed. CONCLUSIONS: Knowledge of the structure further defines the, major epitope and may help in the design of antigen-specific immunotherapy, for treatment of PBC.
About this Structure
1FYC is a Single protein structure of sequence from Homo sapiens. Active as Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the major autoantigen in primary biliary cirrhosis., Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ, Gastroenterology. 1998 Jul;115(1):139-46. PMID:9649469
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