SABER UCV >
1) Investigación >
Artículos Publicados >
Por favor, use este identificador para citar o enlazar este ítem:
http://hdl.handle.net/10872/19559
|
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 |
Aparece en las colecciones: | Artículos Publicados
|
Los ítems de DSpace están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.
|