2ez5
From Proteopedia
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- | [[ | + | ==Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex== |
+ | <StructureSection load='2ez5' size='340' side='right' caption='[[2ez5]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2ez5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EZ5 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ez5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ez5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ez5 RCSB], [http://www.ebi.ac.uk/pdbsum/2ez5 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/2ez5_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Interactions between the WW domains of Drosophila Nedd4 (dNedd4) and Commissureless (Comm) PY motifs promote axon crossing at the CNS midline and muscle synaptogenesis. Here we report the solution structure of the dNedd4 WW3* domain complexed to the second PY motif (227'TGLPSYDEALH237') of Comm. Unexpectedly, there are interactions between WW3* and ligand residues both N- and C-terminal to the PY motif. Residues Y232'-L236' form a helical turn, following the PPII helical PY motif. Mutagenesis and binding studies confirm the importance of these extensive contacts, not simultaneously observed in other WW domain complexes, and identify a variable loop in WW3* responsible for its high-affinity interaction. These studies expand our general understanding of the molecular determinants involved in WW domain-ligand recognition. In addition, they provide insights into the specific regulation of dNedd4-mediated ubiquitination of Comm and subsequent internalization of Comm or the Comm/Roundabout complex, critical for CNS and muscle development. | ||
- | + | Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex.,Kanelis V, Bruce MC, Skrynnikov NR, Rotin D, Forman-Kay JD Structure. 2006 Mar;14(3):543-53. PMID:16531238<ref>PMID:16531238</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: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Bruce, M C.]] | [[Category: Bruce, M C.]] |
Revision as of 00:52, 30 September 2014
Solution Structure of the dNedd4 WW3* Domain- Comm LPSY Peptide Complex
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