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

Jürgen Bosch, Stewart Turley, Thomas M. Daly, Stephen M. Bogh, Michelle L. Villasmil, Claudia Roach, Na Zhou, Joanne M. Morrisey, Akhil B. Vaidya, Lawrence W. Bergman, Wim G J Hol

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)4852-4857
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number13
StatePublished - Mar 28 2006
Externally publishedYes


  • Cell invasion machinery
  • Gliding motility
  • Myosin-tail-interacting protein
  • Plasmodium

ASJC Scopus subject areas

  • Genetics
  • General


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