View source for 2lc7


==Solution structure of the isolated Par-6 PDZ domain==
<StructureSection load='2lc7' size='340' side='right'caption='[[2lc7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LC7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc7 OCA], [https://pdbe.org/2lc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lc7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lc7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O97111_DROME O97111_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Here, we report a novel mechanism of PDZ (PSD-95/Dlg/ZO-1) domain regulation that distorts a conserved element of PDZ ligand recognition. The polarity regulator Par-6 assembles a conserved multiprotein complex and is directly modulated by the Rho GTPase Cdc42. Cdc42 binds the adjacent Cdc42/Rac interactive binding (CRIB) and PDZ domains of Par-6, increasing C-terminal ligand binding affinity by 10-fold. By solving structures of the isolated PDZ domain and a disulfide-stabilized CRIB-PDZ, we detected a conformational switch that controls affinity by altering the configuration of the conserved "GLGF" loop. As a result, lysine 165 is displaced from the PDZ core by an adjacent hydrophobic residue, disrupting coordination of the PDZ ligand-binding cleft. Stabilization of the CRIB:PDZ interface restores K165 to its canonical location in the binding pocket. We conclude that a unique "dipeptide switch" in the Par-6 PDZ transmits a signal for allosteric activation to the ligand-binding pocket.

A Conformational Switch in the CRIB-PDZ Module of Par-6.,Whitney DS, Peterson FC, Volkman BF Structure. 2011 Nov 9;19(11):1711-22. PMID:22078569<ref>PMID:22078569</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lc7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Peterson FC]]
[[Category: Volkman BF]]
[[Category: Whitney DS]]