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In silico identification of the protein disulfide isomerase family from a protozoan parasite ☆

Paper ID Volume ID Publish Year Pages File Format Full-Text
15534 1421 2008 5 PDF Available
Title
In silico identification of the protein disulfide isomerase family from a protozoan parasite ☆
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.

Keywords
PDI, protein disulfide isomerase; Trx, thioredoxin; SNP, single nucleotide polymorphism; ER, endoplasmic reticulumProtozoa; Parasite; Entamoeba histolytica; Protein disulfide isomerase family
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In silico identification of the protein disulfide isomerase family from a protozoan parasite ☆
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Publisher
Database: Elsevier - ScienceDirect
Journal: Computational Biology and Chemistry - Volume 32, Issue 1, February 2008, Pages 67–71
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
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