1ds6

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(New page: 200px<br /> <applet load="1ds6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ds6, resolution 2.35&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1ds6.gif|left|200px]]<br />
 
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<applet load="1ds6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ds6, resolution 2.35&Aring;" />
 
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'''CRYSTAL STRUCTURE OF A RAC-RHOGDI COMPLEX'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF A RAC-RHOGDI COMPLEX==
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Rho family-specific guanine nucleotide dissociation inhibitors (RhoGDIs), decrease the rate of nucleotide dissociation and release Rho proteins such, as RhoA, Rac and Cdc42 from membranes, forming tight complexes that, shuttle between cytosol and membrane compartments. We have solved the, crystal structure of a complex between the RhoGDI homolog LyGDI and, GDP-bound Rac2, which are abundant in leukocytes, representing the, cytosolic, resting pool of Rho species to be activated by extracellular, signals. The N-terminal domain of LyGDI (LyN), which has been reported to, be flexible in isolated RhoGDIs, becomes ordered upon complex formation, and contributes more than 60% to the interface area. The structure is, consistent with the C-terminus of Rac2 binding to a hydrophobic cavity, previously proposed as isoprenyl binding site. An inner segment of LyN, forms a helical hairpin that contacts mainly the switch regions of Rac2., The architecture of the complex interface suggests a mechanism for the, inhibition of guanine nucleotide dissociation that is based on the, stabilization of the magnesium (Mg2+) ion in the nucleotide binding, pocket.
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<StructureSection load='1ds6' size='340' side='right'caption='[[1ds6]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ds6]] 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=1DS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DS6 FirstGlance]. <br>
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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]] 2.35&#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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1ds6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds6 OCA], [https://pdbe.org/1ds6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ds6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ds6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds6 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/RAC2_HUMAN RAC2_HUMAN] Defects in RAC2 are the cause of neutrophil immunodeficiency syndrome (NEUID) [MIM:[https://omim.org/entry/608203 608203].<ref>PMID:10758162</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/RAC2_HUMAN RAC2_HUMAN] Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase.<ref>PMID:1660188</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/ds/1ds6_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/main_output.php?pdb_ID=1ds6 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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Rho family-specific guanine nucleotide dissociation inhibitors (RhoGDIs) decrease the rate of nucleotide dissociation and release Rho proteins such as RhoA, Rac and Cdc42 from membranes, forming tight complexes that shuttle between cytosol and membrane compartments. We have solved the crystal structure of a complex between the RhoGDI homolog LyGDI and GDP-bound Rac2, which are abundant in leukocytes, representing the cytosolic, resting pool of Rho species to be activated by extracellular signals. The N-terminal domain of LyGDI (LyN), which has been reported to be flexible in isolated RhoGDIs, becomes ordered upon complex formation and contributes more than 60% to the interface area. The structure is consistent with the C-terminus of Rac2 binding to a hydrophobic cavity previously proposed as isoprenyl binding site. An inner segment of LyN forms a helical hairpin that contacts mainly the switch regions of Rac2. The architecture of the complex interface suggests a mechanism for the inhibition of guanine nucleotide dissociation that is based on the stabilization of the magnesium (Mg2+) ion in the nucleotide binding pocket.
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==Disease==
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The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI.,Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P Nat Struct Biol. 2000 Feb;7(2):122-6. PMID:10655614<ref>PMID:10655614</ref>
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Known disease associated with this structure: Neutrophil immunodeficiency syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602049 602049]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1DS6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DS6 OCA].
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</div>
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<div class="pdbe-citations 1ds6" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI., Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P, Nat Struct Biol. 2000 Feb;7(2):122-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10655614 10655614]
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*[[Rac 3D structures|Rac 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Gierschik, P.]]
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[[Category: Gierschik P]]
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[[Category: Illenberger, D.]]
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[[Category: Illenberger D]]
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[[Category: Jensen, O.N.]]
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[[Category: Jensen ON]]
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[[Category: Scheffzek, K.]]
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[[Category: Scheffzek K]]
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[[Category: Stephan, I.]]
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[[Category: Stephan I]]
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[[Category: GDP]]
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[[Category: MG]]
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[[Category: beta sandwhich]]
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[[Category: g-domain]]
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[[Category: gtp-binding protein]]
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[[Category: immunoglobulin fold]]
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[[Category: protein-protein complex]]
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[[Category: walker fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:35:19 2007''
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Current revision

CRYSTAL STRUCTURE OF A RAC-RHOGDI COMPLEX

PDB ID 1ds6

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