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1yvd

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[[Image:1yvd.gif|left|200px]]
 
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{{Structure
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==GppNHp-Bound Rab22 GTPase==
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|PDB= 1yvd |SIZE=350|CAPTION= <scene name='initialview01'>1yvd</scene>, resolution 1.93&Aring;
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<StructureSection load='1yvd' size='340' side='right'caption='[[1yvd]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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<table><tr><td colspan='2'>[[1yvd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVD FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.93&#8491;</td></tr>
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|GENE= Rab22a, Rab22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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|DOMAIN=
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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=1yvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvd OCA], [https://pdbe.org/1yvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yvd RCSB], [https://www.ebi.ac.uk/pdbsum/1yvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvd ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvd OCA], [http://www.ebi.ac.uk/pdbsum/1yvd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yvd RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RB22A_MOUSE RB22A_MOUSE] Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth (By similarity). Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form.<ref>PMID:19759177</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/1yvd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1yvd ConSurf].
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<div style="clear:both"></div>
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'''GppNHp-Bound Rab22 GTPase'''
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==See Also==
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*[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]]
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== References ==
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==Overview==
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<references/>
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Rab GTPases regulate all stages of membrane trafficking, including vesicle budding, cargo sorting, transport, tethering and fusion. In the inactive (GDP-bound) conformation, accessory factors facilitate the targeting of Rab GTPases to intracellular compartments. After nucleotide exchange to the active (GTP-bound) conformation, Rab GTPases interact with functionally diverse effectors including lipid kinases, motor proteins and tethering complexes. How effectors distinguish between homologous Rab GTPases represents an unresolved problem with respect to the specificity of vesicular trafficking. Using a structural proteomic approach, we have determined the specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family. The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions. The observed specificity is determined at a family-wide level by structural diversity in the active conformation, which governs the spatial disposition of critical conserved recognition determinants, and by a small number of both positive and negative sequence determinants that allow further discrimination between Rab GTPases with similar switch conformations.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1YVD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVD OCA].
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==Reference==
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Structural basis of family-wide Rab GTPase recognition by rabenosyn-5., Eathiraj S, Pan X, Ritacco C, Lambright DG, Nature. 2005 Jul 21;436(7049):415-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16034420 16034420]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Eathiraj S]]
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[[Category: Eathiraj, S.]]
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[[Category: Lambright DG]]
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[[Category: Lambright, D G.]]
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[[Category: Pan X]]
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[[Category: Pan, X.]]
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[[Category: Ritacco C]]
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[[Category: Ritacco, C.]]
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[[Category: protein transport]]
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[[Category: rab gtpase]]
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[[Category: rab22]]
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[[Category: vesicular trafficking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:24:05 2008''
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Current revision

GppNHp-Bound Rab22 GTPase

PDB ID 1yvd

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