1mhq

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[[Image:1mhq.png|left|200px]]
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==Crystal Structure Of Human GGA2 VHS Domain==
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<StructureSection load='1mhq' size='340' side='right' caption='[[1mhq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mhq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MHQ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mhq RCSB], [http://www.ebi.ac.uk/pdbsum/1mhq PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mh/1mhq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1mhq| PDB=1mhq | SCENE= }}
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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>
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===Crystal Structure Of Human GGA2 VHS Domain===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12606052}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1mhq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHQ OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012606052</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Zhang, X C.]]
[[Category: Zhang, X C.]]

Revision as of 15:12, 28 September 2014

Crystal Structure Of Human GGA2 VHS Domain

1mhq, resolution 2.20Å

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