1i4d: Difference between revisions

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[[Image:1i4d.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED WITH ARFAPTIN (P21)==
|PDB= 1i4d |SIZE=350|CAPTION= <scene name='initialview01'>1i4d</scene>, resolution 2.5&Aring;
<StructureSection load='1i4d' size='340' side='right'caption='[[1i4d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
<table><tr><td colspan='2'>[[1i4d]] is a 3 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=1I4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I4D FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1i4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4d OCA], [https://pdbe.org/1i4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i4d RCSB], [https://www.ebi.ac.uk/pdbsum/1i4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i4d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARFP2_HUMAN ARFP2_HUMAN] Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/1i4d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1i4d ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED WITH ARFAPTIN (P21)'''
==See Also==
 
*[[Rac 3D structures|Rac 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1I4D is a [[Protein complex]] structure of sequences 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=1I4D OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11346801 11346801]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Gamblin, S J.]]
[[Category: Gamblin SJ]]
[[Category: Justin, N.]]
[[Category: Justin N]]
[[Category: Smerdon, S J.]]
[[Category: Smerdon SJ]]
[[Category: Tarricone, C.]]
[[Category: Tarricone C]]
[[Category: Xiao, B.]]
[[Category: Xiao B]]
[[Category: GDP]]
[[Category: MG]]
[[Category: coiled coil]]
[[Category: complex]]
[[Category: g-protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:22 2008''

Latest revision as of 10:32, 7 February 2024

CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED WITH ARFAPTIN (P21)CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP COMPLEXED WITH ARFAPTIN (P21)

Structural highlights

1i4d is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARFP2_HUMAN Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1i4d, resolution 2.50Å

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OCA
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