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==Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD== | ==Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD== | ||
<StructureSection load='4mit' size='340' side='right' caption='[[4mit]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4mit' size='340' side='right' caption='[[4mit]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] </span></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=4mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mit RCSB], [http://www.ebi.ac.uk/pdbsum/4mit PDBsum]</span></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=4mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mit OCA], [http://pdbe.org/4mit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mit RCSB], [http://www.ebi.ac.uk/pdbsum/4mit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mit ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4mit" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:25, 11 August 2016
Crystal structure of E. histolytica RacC bound to the EhPAK4 PBDCrystal structure of E. histolytica RacC bound to the EhPAK4 PBD
Structural highlights
Publication Abstract from PubMedRho family GTPases modulate actin cytoskeleton dynamics by signaling through multiple effectors, including the p21-activated kinases (PAKs). The intestinal parasite Entamoeba histolytica expresses approximately 20 Rho family GTPases and seven isoforms of PAK, two of which have been implicated in pathogenesis-related processes such as amoebic motility and invasion and host cell phagocytosis. Here, we describe two previously unstudied PAK isoforms, EhPAK4 and EhPAK5, as highly specific effectors of EhRacC. A structural model based on 2.35 A X-ray crystallographic data of a complex between EhRacC(Q65L).GTP and the EhPAK4 p21 binding domain (PBD) reveals a fairly well-conserved Rho/effector interface despite deviation of the PBD alpha-helix. A structural comparison with EhRho1 in complex with EhFormin1 suggests likely determinants of Rho family GTPase signaling specificity in E. histolytica. These findings suggest a high degree of Rho family GTPase diversity and specificity in the single-cell parasite E. histolytica. Because PAKs regulate pathogenesis-related processes in E. histolytica, they may be valid pharmacologic targets for anti-amoebiasis drugs. Entamoeba histolytica RacC Selectively Engages p21-Activated Kinase Effectors.,Bosch DE, Siderovski DP Biochemistry. 2015 Jan 20;54(2):404-12. doi: 10.1021/bi501226f. Epub 2015 Jan 2. PMID:25529118[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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