2auc: Difference between revisions

Revision as of 17:31, 21 February 2008

Structure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motor

OverviewOverview

The 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.

About this StructureAbout this Structure

2AUC is a Protein complex structure of sequences from Plasmodium knowlesi. Full crystallographic information is available from OCA.

ReferenceReference

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

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 ==Overview==
-The 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.
+The 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.
 ==About this Structure==
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 [[Category: Protein complex]]
 [[Category: Bosch, J.]]
-[[Category: Hol, W.G.J.]]
+[[Category: Hol, W G.J.]]
-[[Category: SGPP, Structural.Genomics.of.Pathogenic.Protozoa.Consortium.]]
+[[Category: SGPP, Structural Genomics of Pathogenic Protozoa Consortium.]]
 [[Category: Turley, S.]]
 [[Category: myoa]]
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 [[Category: structural genomics of pathogenic protozoa consortium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:10:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:05 2008''