Interaction and dynamics of the Plasmodium falciparum MTIP-MyoA complex, a key component of the invasion motor in the malaria parasite.
The myosin tail domain interacting protein-myosin A (MTIP-MyoA) protein complex is an essential element of the motor driving invasion of red blood cells by the Plasmodium species that cause malaria. Here we report the key determinants of binding at the MTIP/MyoA interface, and the first structural study on the complex in solution using protein NMR.
Thomas
Jemima C
JC
Department of Chemistry, Imperial College London, Exhibition Rd., London, UK SW7 2AZ
Green
Judith L
JL
Howson
Ronald I
RI
Simpson
Peter
P
Moss
David K
DK
Martin
Stephen R
SR
Holder
Anthony A
AA
Cota
Ernesto
E
Tate
Edward W
EW
D000595:Amino Acid Sequence; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D006790:Host-Parasite Interactions / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D009218:Myosins / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010963:Plasmodium falciparum / Q000502:physiology*; D015800:Protozoan Proteins / Q000737:chemistry / Q000378:metabolism*
D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D046912:Multiprotein Complexes; D015800:Protozoan Proteins; D009218:Myosins