4j2c

</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=4j2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j2c OCA], [https://pdbe.org/4j2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j2c RCSB], [https://www.ebi.ac.uk/pdbsum/4j2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j2c ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The Golgi-Associated Retrograde Protein (GARP) complex is a tethering factor involved in the fusion of endosome-derived transport vesicles to the trans-Golgi network through interaction with components of the Syntaxin 6/Syntaxin 16/Vti1a/VAMP4 SNARE complex. The mechanisms by which GARP and other tethering factors engage the SNARE fusion machinery are poorly understood. Herein, we report the structural basis for the interaction of the human Ang2 subunit of GARP with the Syntaxin 6 and the closely related Syntaxin 10. The crystal structure of the Syntaxin 6 Habc domain in complex with a peptide from the N terminus of Ang2 shows a binding mode in which a dityrosine motif of Ang2 interacts with a highly conserved groove in Syntaxin 6. Structure-based mutational analyses validate the crystal structure and support the phylogenetic conservation of this interaction.

Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6.,Abascal-Palacios G, Schindler C, Rojas AL, Bonifacino JS, Hierro A Structure. 2013 Sep 3;21(9):1698-706. doi: 10.1016/j.str.2013.06.025. Epub 2013, Aug 8. PMID:23932592<ref>PMID:23932592</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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