Molecular modelling of epitope presentation using membrane protein OmpC.
Indian J Biochem Biophys
;
2001 Oct; 38(5): 294-7
Article
in English
| IMSEAR
| ID: sea-28005
ABSTRACT
Three-dimensional models of the chimeric S. typhi OmpC protein carrying an epitope from rotavirus VP4 capsid protein on either of two exposed loops (fourth and sixth) were constructed separately, using computer-aided homology modelling. The theoretical model of S. typhi OmpC was used as a template. The monomers were initially energy minimized. The trimers were generated for both the chimeric S. typhi OmpC proteins and the structures were optimized after several cycles of minimization. The surface accessibility calculations for the resulting models show that epitope recognition should be more effective in the fourth loop than in the sixth loop, in accordance with the experimental results on the immunogenic nature of the rotaviral epitope inserted into the two putative loops of S. typhi OmpC.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Protein Conformation
/
Salmonella typhi
/
Bacterial Proteins
/
Molecular Sequence Data
/
Models, Molecular
/
Amino Acid Sequence
/
Porins
/
Antigen Presentation
/
Epitopes
Language:
English
Journal:
Indian J Biochem Biophys
Year:
2001
Type:
Article
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