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<StructureSection load='1pbv' size='340' side='right'caption='[[1pbv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1pbv' size='340' side='right'caption='[[1pbv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pbv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PBV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pbv]] 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=1PBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PBV FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbv OCA], [http://pdbe.org/1pbv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pbv RCSB], [http://www.ebi.ac.uk/pdbsum/1pbv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pbv ProSAT]</span></td></tr>
</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&#8491;</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=1pbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbv OCA], [https://pdbe.org/1pbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pbv RCSB], [https://www.ebi.ac.uk/pdbsum/1pbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pbv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYH2_HUMAN CYH2_HUMAN]] Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane.<ref>PMID:17398095</ref>
[https://www.uniprot.org/uniprot/CYH2_HUMAN CYH2_HUMAN] Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane.<ref>PMID:17398095</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1pbv ConSurf].
</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=1pbv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Small G proteins switch from a resting, GDP-bound state to an active, GTP-bound state. As spontaneous GDP release is slow, guanine-nucleotide-exchange factors (GEFs) are required to promote fast activation of small G proteins through replacement of GDP with GTP in vivo. Families of GEFs with no sequence similarity to other GEF families have now been assigned to most families of small G proteins. In the case of the small G protein Arf1, the exchange of bound GDP for GTP promotes the coating of secretory vesicles in Golgi traffic. An exchange factor for human Arf1, ARNO, and two closely related proteins, named cytohesin 1 and GPS1, have been identified. These three proteins are modular proteins with an amino-terminal coiled-coil, a central Sec7-like domain and a carboxy-terminal pleckstrin homology domain. The Sec7 domain contains the exchange-factor activity. It was first found in Sec7, a yeast protein involved in secretion, and is present in several other proteins, including the yeast exchange factors for Arf, Geal and Gea2. Here we report the crystal structure of the Sec7 domain of human ARNO at 2 A resolution and the identification of the site of interaction of ARNO with Arf.
Structure of the Sec7 domain of the Arf exchange factor ARNO.,Cherfils J, Menetrey J, Mathieu M, Le Bras G, Robineau S, Beraud-Dufour S, Antonny B, Chardin P Nature. 1998 Mar 5;392(6671):101-5. PMID:9510256<ref>PMID:9510256</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pbv" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Antonny, B]]
[[Category: Antonny B]]
[[Category: Beraud-Dufour, S]]
[[Category: Beraud-Dufour S]]
[[Category: Bras, G Le]]
[[Category: Chardin P]]
[[Category: Chardin, P]]
[[Category: Cherfils J]]
[[Category: Cherfils, J]]
[[Category: Le Bras G]]
[[Category: Mathieu, M]]
[[Category: Mathieu M]]
[[Category: Menetrey, J]]
[[Category: Menetrey J]]
[[Category: Robineau, S]]
[[Category: Robineau S]]
[[Category: Arf functional class: guanine nucleotide exchange factor]]
[[Category: Arno]]
[[Category: Exchange factor]]
[[Category: Sec7]]

Latest revision as of 08:06, 14 February 2024

SEC7 DOMAIN OF THE EXCHANGE FACTOR ARNO

1pbv, resolution 2.00Å

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