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6jl7

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(New page: '''Unreleased structure''' The entry 6jl7 is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (09:32, 15 September 2021) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6jl7 is ON HOLD
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==crystal structure of TBC1D23 N terminal domain==
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<StructureSection load='6jl7' size='340' side='right'caption='[[6jl7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6jl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JL7 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TBC1D23, NS4ATP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6jl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jl7 OCA], [https://pdbe.org/6jl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jl7 RCSB], [https://www.ebi.ac.uk/pdbsum/6jl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jl7 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[https://www.uniprot.org/uniprot/TBC23_HUMAN TBC23_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[[https://www.uniprot.org/uniprot/TBC23_HUMAN TBC23_HUMAN]] Putative Rab GTPase-activating protein which plays a role in vesicular trafficking (PubMed:28823707). Involved in endosome-to-Golgi trafficking. Acts as a bridging protein by binding simultaneously to golgins, including GOLGA1 and GOLGA4, located at the trans-Golgi, and to the WASH complex, located on endosome-derived vesicles (PubMed:29084197, PubMed:29426865). Together with WDR11 complex facilitates the golgin-mediated capture of vesicles generated using AP-1 (PubMed:29426865). Plays a role in brain development, including in cortical neuron positioning (By similarity). May also be important for neurite outgrowth, possibly through its involvement in membrane trafficking and cargo delivery, 2 processes that are essential for axonal and dendritic growth (By similarity). May act as a general inhibitor of innate immunity signaling, strongly inhibiting multiple TLR and dectin/CLEC7A-signaling pathways. Does not alter initial activation events, but instead affects maintenance of inflammatory gene expression several hours after bacterial lipopolysaccharide (LPS) challenge (By similarity).[UniProtKB:Q8K0F1]<ref>PMID:28823707</ref> <ref>PMID:29084197</ref> <ref>PMID:29426865</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Members of the Tre2-Bub2-Cdc16 (TBC) family often function to regulate membrane trafficking and to control signaling transductions pathways. As a member of the TBC family, TBC1D23 is critical for endosome-to-Golgi cargo trafficking by serving as a bridge between Golgi-bound golgin-97/245 and the WASH/FAM21 complex on endosomal vesicles. However, the exact mechanisms by which TBC1D23 regulates cargo transport are poorly understood. Here, we present the crystal structure of the N-terminus of TBC1D23 (D23N), which consists of both the TBC and rhodanese domains. We show that the rhodanese domain is unlikely to be an active sulfurtransferase or phosphatase, despite containing a putative catalytic site. Instead, it packs against the TBC domain and forms part of the platform to interact with golgin-97/245. Using the zebrafish model, we show that impacting golgin-97/245-binding, but not the putative catalytic site, impairs neuronal growth and brain development. Altogether, our studies provide structural and functional insights into an essential protein that is required for organelle-specific trafficking and brain development.
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Authors:
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Structure of TBC1D23 N-terminus reveals a novel role for rhodanese domain.,Liu D, Yang F, Liu Z, Wang J, Huang W, Meng W, Billadeau DD, Sun Q, Mo X, Jia D PLoS Biol. 2020 May 26;18(5):e3000746. doi: 10.1371/journal.pbio.3000746., eCollection 2020 May. PMID:32453802<ref>PMID:32453802</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6jl7" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Hu, W]]
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[[Category: Jia, D]]
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[[Category: Sun, Q]]
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[[Category: Bridging factor]]
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[[Category: Protein transport]]
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[[Category: Vesicle transport]]

Current revision

crystal structure of TBC1D23 N terminal domain

PDB ID 6jl7

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