1w3b
From Proteopedia
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| - | [[Image:1w3b.gif|left|200px]]<br /><applet load="1w3b" size=" | + | [[Image:1w3b.gif|left|200px]]<br /><applet load="1w3b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w3b, resolution 2.85Å" /> | caption="1w3b, resolution 2.85Å" /> | ||
'''THE SUPERHELICAL TPR DOMAIN OF O-LINKED GLCNAC TRANSFERASE REVEALS STRUCTURAL SIMILARITIES TO IMPORTIN ALPHA.'''<br /> | '''THE SUPERHELICAL TPR DOMAIN OF O-LINKED GLCNAC TRANSFERASE REVEALS STRUCTURAL SIMILARITIES TO IMPORTIN ALPHA.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1W3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:18:48 2008'' |
Revision as of 08:18, 3 February 2008
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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, peptide-binding site of importin alpha. Based on this structural, similarity, we propose that OGT uses an analogous molecular mechanism to, recognize its targets.
About this Structure
1W3B is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . 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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