In silico identification of the protein disulfide isomerase family from a protozoan parasite.
Comput Biol Chem
; 32(1): 66-70, 2008 Feb.
Article
in En
| MEDLINE
| ID: mdl-17981509
ABSTRACT
Protein disulfide isomerase (PDI) enzymes are eukaryotic oxidoreductases that catalyze the correct formation of disulfide bonds during protein folding. Structurally they are characterized by the presence of functional thioredoxin-like (Trx) domains. For the protozoan parasite causative of the human amebiasis (Entamoeba histolytica), the correct formation of disulfide bonds is important for an accurate folding of its proteins, including some virulence factors. However, little is known about the enzymes involved in this mechanism. We undertook a post-genomic approach to identify the PDI family of this parasite. The genome database survey revealed a set of 11 PDI-encoding sequences with predictable protein thiol/disulfide oxidoreductase activities.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protozoan Proteins
/
Protein Disulfide-Isomerases
/
Entamoeba histolytica
Type of study:
Diagnostic_studies
/
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
Comput Biol Chem
Journal subject:
BIOLOGIA
/
INFORMATICA MEDICA
/
QUIMICA
Year:
2008
Document type:
Article
Affiliation country:
Mexico
Publication country:
ENGLAND
/
ESCOCIA
/
GB
/
GREAT BRITAIN
/
INGLATERRA
/
REINO UNIDO
/
SCOTLAND
/
UK
/
UNITED KINGDOM