1mhq

<table><tr><td colspan='2'>[[1mhq]] is a 2 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=1MHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MHQ FirstGlance]. <br>

</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=1mhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhq OCA], [https://pdbe.org/1mhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhq RCSB], [https://www.ebi.ac.uk/pdbsum/1mhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhq ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/GGA2_HUMAN GGA2_HUMAN]] Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.

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== Publication Abstract from PubMed ==

Golgi-localized, gamma-ear-containing, ARF binding (GGA) proteins regulate intracellular vesicle transport by recognizing sorting signals on the cargo surface in the initial step of the budding process. The VHS (VPS27, Hrs, and STAM) domain of GGA binds with the signal peptides. Here, a crystal structure of the VHS domain of GGA2 is reported at 2.2 A resolution, which permits a direct comparison with that of homologous proteins, GGA1 and GGA3. Significant structural difference is present in the loop between helices 6 and 7, which forms part of the ligand binding pocket. Intrinsic fluorescence spectroscopic study indicates that this loop undergoes a conformational change upon ligand binding. Thus, the current structure suggests that a conformational change induced by ligand binding occurs in this part of the ligand pocket.

Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket.,Zhu G, He X, Zhai P, Terzyan S, Tang J, Zhang XC FEBS Lett. 2003 Feb 27;537(1-3):171-6. PMID:12606052<ref>PMID:12606052</ref>

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

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== References ==

<references/>

[[Category: Human]]

[[Category: Zhang, X C]]

[[Category: Zhu, G]]

[[Category: Super helix]]