1i49

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Current revision (07:32, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1i49' size='340' side='right'caption='[[1i49]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1i49' size='340' side='right'caption='[[1i49]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1i49]] 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=1I49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I49 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1i49]] is a 2 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=1I49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I49 FirstGlance]. <br>
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</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=1i49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i49 OCA], [https://pdbe.org/1i49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i49 RCSB], [https://www.ebi.ac.uk/pdbsum/1i49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i49 ProSAT]</span></td></tr>
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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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i49 OCA], [https://pdbe.org/1i49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i49 RCSB], [https://www.ebi.ac.uk/pdbsum/1i49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i49 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ARFP2_HUMAN ARFP2_HUMAN]] Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling.
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[https://www.uniprot.org/uniprot/ARFP2_HUMAN ARFP2_HUMAN] Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling.
== 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=1i49 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=1i49 ConSurf].
<div style="clear:both"></div>
<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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Small G proteins are GTP-dependent molecular switches that regulate numerous cellular functions. They can be classified into homologous subfamilies that are broadly associated with specific biological processes. Cross-talk between small G-protein families has an important role in signalling, but the mechanism by which it occurs is poorly understood. The coordinated action of Arf and Rho family GTPases is required to regulate many cellular processes including lipid signalling, cell motility and Golgi function. Arfaptin is a ubiquitously expressed protein implicated in mediating cross-talk between Rac (a member of the Rho family) and Arf small GTPases. Here we show that Arfaptin binds specifically to GTP-bound Arf1 and Arf6, but binds to Rac.GTP and Rac.GDP with similar affinities. The X-ray structure of Arfaptin reveals an elongated, crescent-shaped dimer of three-helix coiled-coils. Structures of Arfaptin with Rac bound to either GDP or the slowly hydrolysable analogue GMPPNP show that the switch regions adopt similar conformations in both complexes. Our data highlight fundamental differences between the molecular mechanisms of Rho and Ras family signalling, and suggest a model of Arfaptin-mediated synergy between the Arf and Rho family signalling pathways.
 
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The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways.,Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ Nature. 2001 May 10;411(6834):215-9. PMID:11346801<ref>PMID:11346801</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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<div class="pdbe-citations 1i49" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gamblin, S J]]
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[[Category: Gamblin SJ]]
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[[Category: Justin, N]]
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[[Category: Justin N]]
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[[Category: Smerdon, S J]]
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[[Category: Smerdon SJ]]
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[[Category: Tarricone, C]]
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[[Category: Tarricone C]]
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[[Category: Xiao, B]]
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[[Category: Xiao B]]
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[[Category: Signaling protein]]
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF ARFAPTIN

PDB ID 1i49

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