Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins.

Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Research Abstract Details 

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Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Abstract Text:

T Ferenci,

A stereospecific binding site is not the only determinant governing the selectivity of transport proteins. An understanding of transport across cellular membranes requires a description of the different compartments within a transmembrane channel; evidence for the existence of these compartments comes from the selectivity properties of genetically modified maltoporin. Such compartments may also be of significance in determining the specificity of other transport proteins.

Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Publishing Authors By Initials

T Ferenci,

For similar proteins: membrane proteins: receptors, cell surface: receptors, virus research abstracts see: proteins: membrane proteins: receptors, cell surface: receptors, virus research

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Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Journal Published:

PUBLICATION TYPE: Review

Journal: BioEssays : news and reviews in molecular, cellula

VOLUME: 10

Page Numbers: 3-7

Journal Abbreviation: Bioessays

ISSN: 0265-9247

DAY: 27

MONTH: Jan

YEAR: 1989

Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Information

Number of References: 45

LANGUAGE: eng

NlmUniqueID: 8510851

Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Keywords Mesh Terms:

KEYWORDS: Receptors, Virus

MESH TERMS: metabolism

Chemical & Substance for Abstract: Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. Information

Substance Name: maltoporins

Registry Number: 0

Grant and Affiliation Information for Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins.

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Country: ENGLAND

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MEDLINETA: Bioessays

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Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins Related Publications

• Affinity engineering of maltoporin: variants with enhanced affinity for particular ligands.
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• Combinatorial mutagenesis of the lamB gene: residues 41 through 43, which are conserved in Escherichia coli outer membrane proteins, are informationally important in maltoporin structure and function.
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• Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress.
• Epitope mapping by cysteine mutagenesis: identification of residues involved in recognition by three monoclonal antibodies directed against LamB glycoporin in the outer membrane of Escherichia coli.
• Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure.
• Genetic mapping of starch- and lambda-receptor sites in maltoporin: identification of substitutions causing direct and indirect effects on binding sites by cysteine mutagenesis.
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