Journal article
Structure of the MTIP–MyoA complex, a key component of the malaria parasite invasion motor
Proceedings of the National Academy of Sciences - PNAS, v 103(13), pp 4852-4857
28 Mar 2006
PMID: 16547135
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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.
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Details
- Title
- Structure of the MTIP–MyoA complex, a key component of the malaria parasite invasion motor
- Creators
- Jürgen Bosch - Departments of Biochemistry and Biological Structure andStewart Turley - Departments of Biochemistry and Biological Structure andThomas M Daly - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Stephen M Bogh - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Michelle L Villasmil - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Claudia Roach - Departments of Biochemistry and Biological Structure andNa Zhou - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Joanne M Morrisey - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Akhil B Vaidya - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Lawrence W Bergman - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129Wim G. J Hol - Departments of Biochemistry and Biological Structure and
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 103(13), pp 4852-4857
- Publisher
- National Academy of Sciences
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology; [Retired Faculty]
- Web of Science ID
- WOS:000236472500014
- Scopus ID
- 2-s2.0-33645531531
- Other Identifier
- 991014878192704721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology