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Journal article
The structure of the D3 domain of Plasmodium falciparum myosin tail interacting protein MTIP in complex with a nanobody
Molecular and biochemical parasitology, v 190(2)
Aug 2013
PMID: 23831371
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Abstract
•The crystal structure of a complex of P. falciparum MTIP and an anti-MTIP nanobody.•The third domain of MTIP adopts a more closed conformation than observed so far.•The nanobody binds next to the MyoA helix-binding groove of MTIP.•Compounds targeting MyoA and nanobody binding areas may lead to new antimalarials.
Apicomplexan parasites enter host cells by many sophisticated steps including use of an ATP-powered invasion machinery. The machinery consists of multiple proteins, including a special myosin (MyoA) which moves along an actin fiber and which is connected to the myosin tail interaction protein (MTIP). Here we report a crystal structure of the major MyoA-binding domain (D3) of Plasmodium falciparum MTIP in complex with an anti-MTIP nanobody. In this complex, the MyoA-binding groove in MTIP-D3 is considerably less accessible than when occupied by the MyoA helix, due to a shift of two helices. The nanobody binds to an area slightly overlapping with the MyoA binding groove, covering a hydrophobic region next to the groove entrance. This provides a new avenue for arriving at compounds interfering with the invasion machinery since small molecules binding simultaneously to the nanobody binding site and the adjacent MyoA binding groove would prevent MyoA binding by MTIP.
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Details
- Title
- The structure of the D3 domain of Plasmodium falciparum myosin tail interacting protein MTIP in complex with a nanobody
- Creators
- Susmita Khamrui - Department of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, Seattle, WA 98195, United StatesStewart Turley - Department of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, Seattle, WA 98195, United StatesEls Pardon - Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, BelgiumJan Steyaert - Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, BelgiumErkang Fan - Department of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, Seattle, WA 98195, United StatesChristophe L.M.J Verlinde - Department of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, Seattle, WA 98195, United StatesLawrence W Bergman - Center for Molecular Parasitology, Department of Microbiology and Immunology, Drexel University College of Medicine, Philadelphia, PA 19129, United StatesWim G.J Hol - Department of Biochemistry, Biomolecular Structure Center, School of Medicine, University of Washington, Seattle, WA 98195, United States
- Publication Details
- Molecular and biochemical parasitology, v 190(2)
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:000324226300007
- Scopus ID
- 2-s2.0-84880998541
- Other Identifier
- 991014877965204721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Parasitology