1z0a: Difference between revisions

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 <StructureSection load='1z0a' size='340' side='right'caption='[[1z0a]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z0a]] 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=1Z0A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z0A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z0a]] is a 4 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=1Z0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0A FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAB2, RAB2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0a OCA], [http://pdbe.org/1z0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0a RCSB], [http://www.ebi.ac.uk/pdbsum/1z0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0a 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=1z0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0a OCA], [https://pdbe.org/1z0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0a RCSB], [https://www.ebi.ac.uk/pdbsum/1z0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RAB2A_HUMAN RAB2A_HUMAN]] Required for protein transport from the endoplasmic reticulum to the Golgi complex.
+[https://www.uniprot.org/uniprot/RAB2A_HUMAN RAB2A_HUMAN] Required for protein transport from the endoplasmic reticulum to the Golgi complex.
 == Evolutionary Conservation ==
 [[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=1z0a ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:16034420<ref>PMID:16034420</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1z0a" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Eathiraj, S]]
+[[Category: Eathiraj S]]
-[[Category: Lambright, D G]]
+[[Category: Lambright DG]]
-[[Category: Pan, X]]
+[[Category: Pan X]]
-[[Category: Ritacco, C]]
+[[Category: Ritacco C]]
-[[Category: Protein transport]]
-[[Category: Rab gtpase]]
-[[Category: Rab2]]
-[[Category: Vesicular trafficking]]