This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2lc6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:31, 18 January 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Solution structure of Par-6 Q144C/L164C==
==Solution structure of Par-6 Q144C/L164C==
-
<StructureSection load='2lc6' size='340' side='right' caption='[[2lc6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+
<StructureSection load='2lc6' size='340' side='right'caption='[[2lc6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
[[2lc6]] is a 1 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=2LC6 OCA]. <br>
+
<table><tr><td colspan='2'>[[2lc6]] 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=2LC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LC6 FirstGlance]. <br>
-
<b>[[Related_structure|Related:]]</b> [[2lc7|2lc7]]<br>
+
</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=2lc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc6 OCA], [https://pdbe.org/2lc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lc6 RCSB], [https://www.ebi.ac.uk/pdbsum/2lc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lc6 ProSAT]</span></td></tr>
-
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
+
</table>
-
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lc6 RCSB], [http://www.ebi.ac.uk/pdbsum/2lc6 PDBsum]</span><br>
+
== Function ==
 +
[https://www.uniprot.org/uniprot/O97111_DROME O97111_DROME]
 +
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== 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.
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.
Line 11: Line 14:
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>
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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2lc6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 17: Line 22:
</StructureSection>
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
-
[[Category: Peterson, F C.]]
+
[[Category: Large Structures]]
-
[[Category: Volkman, B F.]]
+
[[Category: Peterson FC]]
-
[[Category: Whitney, D S.]]
+
[[Category: Volkman BF]]
-
[[Category: Cdc42]]
+
[[Category: Whitney DS]]
-
[[Category: Cell adhesion]]
+
-
[[Category: Crib]]
+
-
[[Category: Pdz domain]]
+

Current revision

Solution structure of Par-6 Q144C/L164C

PDB ID 2lc6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools