6if3

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<StructureSection load='6if3' size='340' side='right'caption='[[6if3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6if3' size='340' side='right'caption='[[6if3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6if3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IF3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6if3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IF3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<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=6if3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6if3 OCA], [http://pdbe.org/6if3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6if3 RCSB], [http://www.ebi.ac.uk/pdbsum/6if3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6if3 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6if3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6if3 OCA], [https://pdbe.org/6if3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6if3 RCSB], [https://www.ebi.ac.uk/pdbsum/6if3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6if3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACAP2_HUMAN ACAP2_HUMAN]] GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).<ref>PMID:11062263</ref> [[http://www.uniprot.org/uniprot/RAB35_HUMAN RAB35_HUMAN]] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth.<ref>PMID:16950109</ref> <ref>PMID:21951725</ref>
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[https://www.uniprot.org/uniprot/ACAP2_HUMAN ACAP2_HUMAN] GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).<ref>PMID:11062263</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rab35, a master regulator of membrane trafficking, regulates diverse cellular processes and is associated with various human diseases. Although a number of effectors have been identified, the molecular basis of Rab35-effector interactions remains unclear. Here, we provide the high-resolution crystal structures of Rab35 in complex with its two specific effectors ACAP2 and RUSC2, respectively. In the Rab35/ACAP2 complex structure, Rab35 binds to the terminal ankyrin repeat and a C-terminal extended alpha helix of ACAP2, revealing a previously uncharacterized binding mode both for Rabs and ankyrin repeats. In the Rab35/RUSC2 complex structure, Arg1015 of RUSC2 functions as a "pseudo-arginine finger" that stabilizes the GTP-bound Rab35, thus facilitating the assembly of Rab35/RUSC2 complex. The structural analysis allows us to design specific Rab35 mutants capable of eliminating Rab35/ACAP2 and Rab35/RUSC2 interactions, but not interfering with other effector bindings. The atomic structures also offer possible explanations to disease-associated mutants identified at the Rab35-effector interfaces.
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Rab35/ACAP2 and Rab35/RUSC2 Complex Structures Reveal Molecular Basis for Effector Recognition by Rab35 GTPase.,Lin L, Shi Y, Wang M, Wang C, Zhu J, Zhang R Structure. 2019 Mar 11. pii: S0969-2126(19)30078-4. doi:, 10.1016/j.str.2019.02.008. PMID:30905672<ref>PMID:30905672</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6if3" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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*[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lin, L]]
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[[Category: Lin L]]
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[[Category: Zhang, R]]
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[[Category: Zhang R]]
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[[Category: Zhu, J]]
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[[Category: Zhu J]]
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[[Category: Acap2]]
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[[Category: Complex]]
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[[Category: Cryatal structure]]
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[[Category: Endocytosis]]
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[[Category: Rab35]]
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Current revision

Complex structure of Rab35 and its effector ACAP2

PDB ID 6if3

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OCA

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