title: Structure of C-terminal fragment of merozoite surface protein-1 from Plasmodium vivax determined by homology modeling and molecular dynamics refinement.
abstract: 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-1(19) and PvMSP-1(33) have succeeded in protecting monkeys and a large proportion of individuals, naturally exposed to P. vivax transmission, develop specific antibodies to PvMSP-1(19). This study presents a model for the three-dimensional structure of the C-terminal 19kDa fragment of P. vivax MSP-1 determined by means of homology modeling and molecular dynamics refinement. The structure proved to be consistent with MSP-1(19) 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-1(19) Belem strain were also inspected. Our model is currently used as a basis to understand antibody interactions with PvMSP-1(19).
authors.affiliation: Laboratorio de Modelado Molecular, Unidad de Química Medicinal, Facultad de Farmacia, Universidad Central de Venezuela, Caracas 1041-A, Venezuela. serranol@ucv.ve
authors.forename: María Luisa
authors.initials: ML
authors.lastname: Serrano
authors.forename: Hilda A
authors.initials: HA
authors.lastname: Pérez
authors.forename: J D
authors.initials: JD
authors.lastname: Medina
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D016780:Malaria, Vivax; D020066:Merozoite Surface Protein 1 / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010966:Plasmodium vivax / Q000302:isolation & purification*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D020066:Merozoite Surface Protein 1