1naf

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{{Seed}}
 
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[[Image:1naf.png|left|200px]]
 
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==Crystal structure of the human GGA1 GAT domain==
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The line below this paragraph, containing "STRUCTURE_1naf", creates the "Structure Box" on the page.
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<StructureSection load='1naf' size='340' side='right'caption='[[1naf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1naf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NAF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1naf| PDB=1naf | SCENE= }}
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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=1naf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1naf OCA], [https://pdbe.org/1naf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1naf RCSB], [https://www.ebi.ac.uk/pdbsum/1naf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1naf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GGA1_HUMAN GGA1_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.<ref>PMID:11301005</ref>
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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/na/1naf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1naf 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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The GGAs are a family of clathrin adaptor proteins involved in vesicular transport between the trans-Golgi network and endosomal system. Here we confirm reports that GGAs are targeted to the Golgi via interaction between the GGA-GAT domain and ARF-GTP, and we present the structure of the GAT domain of human GGA1, completing the structural description of the folded domains of GGA proteins. The GGA-GAT domain possesses an all alpha-helical fold with a "paper clip" topology comprising two independent subdomains. Structure-based mutagenesis demonstrates that ARF1-GTP binding by GGAs is exclusively governed by the N-terminal "hook" subdomain, and, using an in vitro recruitment assay, we show that ARF-GTP binding by this small structure is required and sufficient for Golgi targeting of GGAs.
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===crystal structure of the human GGA1 GAT domain===
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The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs.,Collins BM, Watson PJ, Owen DJ Dev Cell. 2003 Mar;4(3):321-32. PMID:12636914<ref>PMID:12636914</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_12636914}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1naf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12636914 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12636914}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1NAF is a [[Single protein]] structure of 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=1NAF OCA].
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==Reference==
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The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs., Collins BM, Watson PJ, Owen DJ, Dev Cell. 2003 Mar;4(3):321-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12636914 12636914]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Collins, B M.]]
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[[Category: Collins BM]]
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[[Category: Owen, D J.]]
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[[Category: Owen DJ]]
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[[Category: Watson, P J.]]
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[[Category: Watson PJ]]
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[[Category: Clathrin-adaptor]]
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[[Category: Gat domain]]
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[[Category: Gga]]
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[[Category: Helical paper-clip]]
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[[Category: Three-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:45:11 2008''
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Current revision

Crystal structure of the human GGA1 GAT domain

PDB ID 1naf

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OCA

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