Saber UCV
Repositorio Institucional
Repositorio Institucional
Please use this identifier to cite or link to this item:
https://saber.ucv.ve/handle/10872/19559
|
| Title: | Structure of C‐terminal fragment of Merozoite Surface Protein‐1 from Plasmodium vivax Determined by Homology Modelling and Molecular Dynamics Refinement |
| Authors: | Serrano, Maria Luisa Medina, JD Perez, Hilda A |
| Keywords: | Homology modeling Molecular dynamics Malaria P. vivax MSP-119 |
| Issue Date: | 11-Jan-2019 |
| Series/Report no.: | Bioorganic & Medicinal Chemistry;2006, 14, 8359‐8365. |
| 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-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 |
| Appears in Collections: | Artículos Publicados |
Files in This Item:
|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.