4n3z: Difference between revisions

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-'''Unreleased structure'''
+==Crystal structure of Rabex-5delta and Rabaptin-5C21 complex==
+<StructureSection load='4n3z' size='340' side='right' caption='[[4n3z]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4n3z]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N3Z FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n3x|4n3x]], [[4n3y|4n3y]]</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=4n3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n3z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n3z RCSB], [http://www.ebi.ac.uk/pdbsum/4n3z 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 4n3z 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-5delta 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]]