2auc: Difference between revisions
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<StructureSection load='2auc' size='340' side='right' caption='[[2auc]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2auc' size='340' side='right' caption='[[2auc]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2auc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2auc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Plakn Plakn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AUC FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene></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=2auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2auc RCSB], [http://www.ebi.ac.uk/pdbsum/2auc 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=2auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2auc OCA], [http://pdbe.org/2auc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2auc RCSB], [http://www.ebi.ac.uk/pdbsum/2auc PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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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 2auc" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Plakn]] | ||
[[Category: Bosch, J]] | [[Category: Bosch, J]] | ||
[[Category: Hol, W G.J]] | [[Category: Hol, W G.J]] | ||
Revision as of 08:19, 10 September 2015
Structure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motorStructure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motor
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials. Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor.,Bosch J, Turley S, Daly TM, Bogh SM, Villasmil ML, Roach C, Zhou N, Morrisey JM, Vaidya AB, Bergman LW, Hol WG Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4852-7. Epub 2006 Mar 17. PMID:16547135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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