5i7z: Difference between revisions

Line 10:

== Function ==

[https://www.uniprot.org/uniprot/O97111_DROME O97111_DROME]

~~<div style="background-color:#fffaf0;">~~

~~== Publication Abstract from PubMed ==~~

Par-6 is a scaffold protein that organizes other proteins into a complex required to initiate and maintain cell polarity. Cdc42-GTP binds the CRIB module of Par-6 and alters the binding affinity of the adjoining PDZ domain. Allosteric regulation of the Par-6 PDZ domain was first demonstrated using a peptide identified in a screen of typical carboxyl-terminal ligands. Crumbs, a membrane protein that localizes a conserved polarity complex, was subsequently identified as a functional partner for Par-6 that likely interacts with the PDZ domain. Here we show by nuclear magnetic resonance that Par-6 binds a Crumbs carboxyl-terminal peptide and report the crystal structure of the PDZ-peptide complex. The Crumbs peptide binds Par-6 more tightly than the previously studied carboxyl peptide ligand and interacts with the CRIB-PDZ module in a Cdc42-dependent manner. The Crumbs:Par-6 crystal structure reveals specific PDZ-peptide contacts that contribute to its higher affinity and Cdc42-enhanced binding. Comparisons with existing structures suggest that multiple C-terminal Par-6 ligands respond to a common conformational switch that transmits the allosteric effects of GTPase binding.

Binding of Crumbs to the Par-6 CRIB-PDZ Module Is Regulated by Cdc42.,Whitney DS, Peterson FC, Kittell AW, Egner JM, Prehoda KE, Volkman BF Biochemistry. 2016 Mar 15;55(10):1455-61. doi: 10.1021/acs.biochem.5b01342. Epub , 2016 Mar 3. PMID:26894406<ref>PMID:26894406</ref>

~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~

~~</div>~~

~~<div class="pdbe-citations 5i7z" style="background-color:#fffaf0;"></div>~~

~~== References ==~~

~~<references/>~~

__TOC__

</StructureSection>

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 10: / Line 10: @@
 == Function ==
 [https://www.uniprot.org/uniprot/O97111_DROME O97111_DROME]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Par-6 is a scaffold protein that organizes other proteins into a complex required to initiate and maintain cell polarity. Cdc42-GTP binds the CRIB module of Par-6 and alters the binding affinity of the adjoining PDZ domain. Allosteric regulation of the Par-6 PDZ domain was first demonstrated using a peptide identified in a screen of typical carboxyl-terminal ligands. Crumbs, a membrane protein that localizes a conserved polarity complex, was subsequently identified as a functional partner for Par-6 that likely interacts with the PDZ domain. Here we show by nuclear magnetic resonance that Par-6 binds a Crumbs carboxyl-terminal peptide and report the crystal structure of the PDZ-peptide complex. The Crumbs peptide binds Par-6 more tightly than the previously studied carboxyl peptide ligand and interacts with the CRIB-PDZ module in a Cdc42-dependent manner. The Crumbs:Par-6 crystal structure reveals specific PDZ-peptide contacts that contribute to its higher affinity and Cdc42-enhanced binding. Comparisons with existing structures suggest that multiple C-terminal Par-6 ligands respond to a common conformational switch that transmits the allosteric effects of GTPase binding.
-Binding of Crumbs to the Par-6 CRIB-PDZ Module Is Regulated by Cdc42.,Whitney DS, Peterson FC, Kittell AW, Egner JM, Prehoda KE, Volkman BF Biochemistry. 2016 Mar 15;55(10):1455-61. doi: 10.1021/acs.biochem.5b01342. Epub , 2016 Mar 3. PMID:26894406<ref>PMID:26894406</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5i7z" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>