Selectivity in solute transport: binding sites and channel structure in maltoporin and other bacterial sugar transport proteins.
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.
Ferenci
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D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D010582:Bacteriophage lambda / Q000378:metabolism; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D018272:Porins; D011991:Receptors, Virus / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins