Structure of C-terminal fragment of merozoite surface protein-1 from Plasmodium vivax determined by homology modeling and molecular dynamics refinement.

Bioorg Med Chem

Laboratorio de Modelado Molecular, Unidad de Química Medicinal, Facultad de Farmacia, Universidad Central de Venezuela, Caracas 1041-A, Venezuela.

Published: December 2006

AI Article Synopsis

  • Current vaccine candidate against Plasmodium vivax is the major merozoite surface protein-1 (PvMSP-1), focusing on its asexual blood stage.
  • Vaccine trials have shown that PvMSP-1(19) can protect monkeys, and many people exposed to P. vivax develop antibodies to this protein.
  • A new 3D model of the C-terminal 19kDa fragment of PvMSP-1 was created, revealing a binding pocket for protein interactions and serving as a framework for studying how antibodies connect with PvMSP-1(19).

Article 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).

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.bmc.2006.09.005DOI Listing

Publication Analysis

Top Keywords

structure c-terminal
8
merozoite surface
8
surface protein-1
8
plasmodium vivax
8
determined homology
8
homology modeling
8
modeling molecular
8
molecular dynamics
8
dynamics refinement
8
vivax
5

Similar Publications

Ergosterol alleviates hepatic steatosis and insulin resistance via promoting fatty acid β-oxidation by activating mitochondrial ACSL1.

Cell Rep

January 2025

State Key Laboratory of Natural Medicines, School of Traditional Chinese Pharmacy, China Pharmaceutical University, Nanjing, Jiangsu, China. Electronic address:

Sterols target sterol-sensing domain (SSD) proteins to lower cholesterol and circulating and hepatic triglyceride levels, but the mechanism remains unclear. In this study, we identify acyl-coenzyme A (CoA) synthetase long-chain family member 1 (ACSL1) as a direct target of ergosterol (ES). The C-terminal domain of ACSL1 undergoes conformational changes from closed to open, and ES may target the drug-binding pocket in the acetyl-CoA synthetase-like domain 1 (ASLD1) of ACSL1 to stabilize the closed conformation and maintain its activity.

View Article and Find Full Text PDF

Among all photosynthetic life forms, cyanobacteria exclusively possess a water-soluble, light-sensitive carotenoprotein complex known as orange carotenoid proteins (OCPs), crucial for their photoprotective mechanisms. These protein complexes exhibit both structural and functional modularity, with distinct C-terminal (CTD) and N-terminal domains (NTD) serving as light-responsive sensor and effector regions, respectively. The majority of cyanobacterial genomes contain genes for OCP homologs and related proteins, highlighting their essential role in survival of the organism over time.

View Article and Find Full Text PDF

Halorhodospira (Hlr.) halophila strain BN9622 is an extremely halophilic and alkaliphilic purple phototrophic bacterium and has been widely used as a model for exploring the osmoadaptive and photosynthetic strategies employed by phototrophic extreme halophiles that enable them to thrive in hypersaline environments. Here we present the cryo-EM structures of (1) a unique native Hlr.

View Article and Find Full Text PDF

O-Methyldehydroserine, ΔSer(Me), is a non-standard α,β-dehydroamino acid, which occurs naturally in Cyrmenins with potential pharmaceutical application. The C-terminal part and the side chain of the ΔSer(Me) residue constitute the β-methoxyacrylate unit, responsible for antifungal activity of Cyrmenins. The short model, Ac-ΔSer(Me)-OMe, was analyzed considering the geometrical isomer Z () and E ().

View Article and Find Full Text PDF

HSP70 chaperones play pivotal roles in facilitating protein folding, refolding, and disaggregation through their binding and releasing activities. This intricate process is further supported by J-domain proteins (JDPs), also known as DNAJs or HSP40s, which can be categorized into classes A and B. In yeast, these classes are represented by Ydj1 and Sis1, respectively.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!