1yvd

<StructureSection load='1yvd' size='340' side='right' caption='[[1yvd]], [[Resolution|resolution]] 1.93&Aring;' scene=''>

<table><tr><td colspan='2'>[[1yvd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YVD FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rab22a, Rab22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=1yvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvd OCA], [http://pdbe.org/1yvd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yvd RCSB], [http://www.ebi.ac.uk/pdbsum/1yvd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvd ProSAT]</span></td></tr>

[[http://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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== 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>

 

[[Category: Lk3 transgenic mice]]

[[Category: Eathiraj, S]]

[[Category: Lambright, D G]]

[[Category: Pan, X]]

[[Category: Ritacco, C]]

[[Category: Vesicular trafficking]]