1lv0

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Current revision (07:36, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1lv0' size='340' side='right'caption='[[1lv0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1lv0' size='340' side='right'caption='[[1lv0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1lv0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LV0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1lv0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LV0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GER:GERAN-8-YL+GERAN'>GER</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d5t|1d5t]], [[1gnd|1gnd]]</div></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=GER:GERAN-8-YL+GERAN'>GER</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1lv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lv0 OCA], [https://pdbe.org/1lv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1lv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lv0 ProSAT]</span></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=1lv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lv0 OCA], [https://pdbe.org/1lv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1lv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lv0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GDIA_BOVIN GDIA_BOVIN]] Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
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[https://www.uniprot.org/uniprot/GDIA_BOVIN GDIA_BOVIN] Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lv0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lv0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Rab GTPases, key regulators of membrane targeting and fusion, require the covalent attachment of geranylgeranyl lipids to their C terminus for function. To elucidate the role of lipid in Rab recycling, we have determined the crystal structure of Rab guanine nucleotide dissociation inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand (H(2)N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding platform in a shallow hydrophobic groove. Mutation of the binding pocket in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to promote release of the GDI-Rab[GDP] complex from the membrane.
 
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Geranylgeranyl switching regulates GDI-Rab GTPase recycling.,An Y, Shao Y, Alory C, Matteson J, Sakisaka T, Chen W, Gibbs RA, Wilson IA, Balch WE Structure. 2003 Mar;11(3):347-57. PMID:12623022<ref>PMID:12623022</ref>
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==See Also==
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*[[Guanine nucleotide dissociation inhibitor|Guanine nucleotide dissociation inhibitor]]
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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 1lv0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bovin]]
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[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alory, C]]
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[[Category: Alory C]]
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[[Category: An, Y]]
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[[Category: An Y]]
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[[Category: Balch, W E]]
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[[Category: Balch WE]]
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[[Category: Chen, W]]
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[[Category: Chen W]]
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[[Category: Gibbs, R A]]
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[[Category: Gibbs RA]]
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[[Category: Matteson, J]]
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[[Category: Matteson J]]
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[[Category: Sakisaka, T]]
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[[Category: Sakisaka T]]
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[[Category: Shao, Y]]
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[[Category: Shao Y]]
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[[Category: Wilson, I A]]
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[[Category: Wilson IA]]
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[[Category: Protein-ligand complex]]
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[[Category: Signaling protein]]
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Current revision

Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide

PDB ID 1lv0

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