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.


4n3y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
==Crystal structure of Rabex-5CC and Rabaptin-5C21 complex==
 +
<StructureSection load='4n3y' size='340' side='right' caption='[[4n3y]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4n3y]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N3Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N3Y FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n3x|4n3x]], [[4n3z|4n3z]]</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=4n3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n3y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n3y RCSB], [http://www.ebi.ac.uk/pdbsum/4n3y PDBsum]</span></td></tr>
 +
<table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Rabex-5 and Rabaptin-5 function together to activate Rab5 and further promote early endosomal fusion in endocytosis. The Rabex-5 GEF activity is autoinhibited by the Rabex-5 CC domain (Rabex-5CC) and activated by the Rabaptin-5 C2-1 domain (Rabaptin-5C21) with yet unknown mechanism. We report here the crystal structures of Rabex-5 in complex with the dimeric Rabaptin-5C21 (Rabaptin-5C212) and in complex with Rabaptin-5C212 and Rab5, along with biophysical and biochemical analyses. We show that Rabex-5CC assumes an amphipathic alpha-helix which binds weakly to the substrate-binding site of the GEF domain, leading to weak autoinhibition of the GEF activity. Binding of Rabaptin-5C21 to Rabex-5 displaces Rabex-5CC to yield a largely exposed substrate-binding site, leading to release of the GEF activity. In the ternary complex the substrate-binding site of Rabex-5 is completely exposed to bind and activate Rab5. Our results reveal the molecular mechanism for the regulation of the Rabex-5 GEF activity.
-
The entry 4n3y is ON HOLD until Paper Publication
+
Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5.,Zhang Z, Zhang T, Wang S, Gong Z, Tang C, Chen J, Ding J Elife (Cambridge). 2014 Jun 23:e02687. doi: 10.7554/eLife.02687. PMID:24957337<ref>PMID:24957337</ref>
-
Authors: Zhang, Z., Zhang, T., Ding, J.
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
Description: Crystal structure of Rabex-5CC and Rabaptin-5C21 complex
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Ding, J.]]
 +
[[Category: Zhang, T.]]
 +
[[Category: Zhang, Z.]]
 +
[[Category: Early endosome]]
 +
[[Category: Endocytosis]]
 +
[[Category: Gef activity]]
 +
[[Category: Rab5]]
 +
[[Category: Rabaptin-5]]
 +
[[Category: Rabex-5]]

Revision as of 08:01, 23 July 2014

Crystal structure of Rabex-5CC and Rabaptin-5C21 complex

4n3y, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n3y"
Views
Personal tools
Navigation
Toolbox