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 PubMed
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.
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
- ↑ Bosch J, Turley S, Daly TM, Bogh SM, Villasmil ML, Roach C, Zhou N, Morrisey JM, Vaidya AB, Bergman LW, Hol WG. Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor. Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4852-7. Epub 2006 Mar 17. PMID:16547135
