4n3x: Difference between revisions
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==Crystal structure of Rabex-5 CC domain== | ==Crystal structure of Rabex-5 CC domain== | ||
<StructureSection load='4n3x' size='340' side='right' caption='[[4n3x]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4n3x' size='340' side='right' caption='[[4n3x]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4n3x]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N3X FirstGlance]. <br> | <table><tr><td colspan='2'>[[4n3x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N3X FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n3y|4n3y]], [[4n3z|4n3z]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n3y|4n3y]], [[4n3z|4n3z]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n3x OCA], [http://pdbe.org/4n3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n3x RCSB], [http://www.ebi.ac.uk/pdbsum/4n3x PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RABEX5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n3x OCA], [http://pdbe.org/4n3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n3x RCSB], [http://www.ebi.ac.uk/pdbsum/4n3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n3x ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4n3x" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4n3x" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Ding, J]] | [[Category: Ding, J]] | ||
[[Category: Zhang, T]] | [[Category: Zhang, T]] | ||
Revision as of 13:01, 15 November 2017
Crystal structure of Rabex-5 CC domainCrystal structure of Rabex-5 CC domain
Structural highlights
Function[RABX5_HUMAN] Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity).[1] [2] [3] Publication Abstract from PubMedRabex-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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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