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Título : Structure of C‐terminal fragment of Merozoite Surface Protein‐1 from Plasmodium vivax Determined by Homology Modelling and Molecular Dynamics Refinement
Autor : Serrano, Maria Luisa
Medina, JD
Perez, Hilda A
Palabras clave : Homology modeling
Molecular dynamics
Malaria P. vivax
MSP-119
Fecha de publicación : 11-Jan-2019
Citación : Bioorganic & Medicinal Chemistry;2006, 14, 8359‐8365.
Resumen : One current vaccine candidate against Plasmodium vivax targeting asexual blood stage is the major merozoite surface protein- 1 of P. vivax (PvMSP-1). Vaccine trials with PvMSP-119 and PvMSP-133 have succeeded in protecting monkeys and a large proportion of individuals, naturally exposed to P. vivax transmission, develop specific antibodies to PvMSP-119. This study presents a model for the three-dimensional structure of the C-terminal 19 kDa fragment of P. vivax MSP-1 determined by means of homology modeling and molecular dynamics refinement. The structure proved to be consistent with MSP-119 of known crystal or solution structures. The presence of a main binding pocket, well suited for protein–protein interactions, was determined by CASTp. Corrections reported to the sequence of PvMSP-119 Belem strain were also inspected. Our model is currently used as a basis to understand antibody interactions with PvMSP-119.
URI : http://hdl.handle.net/10872/19559
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