1w3b
From Proteopedia
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 14:18, 30 October 2007
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THE SUPERHELICAL TPR DOMAIN OF O-LINKED GLCNAC TRANSFERASE REVEALS STRUCTURAL SIMILARITIES TO IMPORTIN ALPHA.
Overview
Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of, intracellular glycosylation catalyzed by the conserved O-linked GlcNAc, transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide, (TPR) repeats that mediates the recognition of a broad range of target, proteins. Components of the nuclear pore complex are major OGT targets, as, OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc, modification at the nuclear envelope. To gain insight into the mechanism, of target recognition, we solved the crystal structure of the homodimeric, TPR domain of human OGT, which contains 11.5 TPR repeats. The repeats form, an elongated superhelix. The concave surface of the superhelix is lined by, absolutely conserved asparagines, in a manner reminiscent of the, ... [(full description)]
About this Structure
1W3B is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha., Jinek M, Rehwinkel J, Lazarus BD, Izaurralde E, Hanover JA, Conti E, Nat Struct Mol Biol. 2004 Oct;11(10):1001-7. Epub 2004 Sep 12. PMID:15361863
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