Analysis and modeling of heat-labile enterotoxins of Escherichia coli suggests a novel space with insights into receptor preference.

doi:10.1080/07391102.2014.974073

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Article

Analysis and modeling of heat-labile enterotoxins of Escherichia coli suggests a novel space with insights into receptor preference.

Journal of biomolecular structure & dynamics - 1 Jan 2015

Krishna Raja M, Ghosh Asit Ranjan, Vino S, Sajitha Lulu S

Abstract excerpt

Features of heat-labile enterotoxins of Escherichia coli which make them fit to use as novel receptors for antidiarrheals are not completely explored. Data-set of 14 different serovars of enterotoxigenic Escherichia coli producing heat-labile toxins were taken from NCBI Genbank database and used in the study. Sequence analysis showed mutations in different subunits and also at their interface residues. As these...

Topics

Amino Acid Sequence
Amino Acid Substitution
Bacterial Toxins
Binding Sites
Enterotoxins
Escherichia coli Proteins
Humans
Ligands
Models, Molecular
Molecular Docking Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Dynamics Simulation

Molecular Sequence Data

Mutation

Phylogeny

Protein Binding

Protein Interaction Domains and Motifs

Protein Subunits

Quantitative Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 25375068
DOI: 10.1080/07391102.2014.974073

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