2xbb
From Proteopedia
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| - | [[ | + | ==NEDD4 HECT:UB COMPLEX== |
| + | <StructureSection load='2xbb' size='340' side='right' caption='[[2xbb]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xbb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XBB FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xbf|2xbf]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xbb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xbb RCSB], [http://www.ebi.ac.uk/pdbsum/2xbb PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Several mechanisms have been proposed for the synthesis of substrate-linked ubiquitin chains. HECT ligases directly catalyse protein ubiquitination and have been found to non-covalently interact with ubiquitin. We report crystal structures of the Nedd4 HECT domain, alone and in complex with ubiquitin, which show a new binding mode involving two surfaces on ubiquitin and both subdomains of the HECT N-lobe. The structures suggest a model for HECT-to-substrate ubiquitin transfer, in which the growing chain on the substrate is kept close to the catalytic cysteine to promote processivity. Mutational analysis highlights differences between the processes of substrate polyubiquitination and self-ubiquitination. | ||
| - | + | Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation.,Maspero E, Mari S, Valentini E, Musacchio A, Fish A, Pasqualato S, Polo S EMBO Rep. 2011 Mar 11. PMID:21399620<ref>PMID:21399620</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Ubiquitin protein ligase|Ubiquitin protein ligase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Cecatiello, V | + | [[Category: Cecatiello, V]] |
| - | [[Category: Maspero, E | + | [[Category: Maspero, E]] |
| - | [[Category: Musacchio, A | + | [[Category: Musacchio, A]] |
| - | [[Category: Pasqualato, S | + | [[Category: Pasqualato, S]] |
| - | [[Category: Polo, S | + | [[Category: Polo, S]] |
[[Category: Ligase-protein binding complex]] | [[Category: Ligase-protein binding complex]] | ||
Revision as of 08:38, 26 November 2014
NEDD4 HECT:UB COMPLEX
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