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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/11637
Title: A biophysical glance at the outer surface of the membrane transporter SGLT1
Authors: Navneet K. Tyagi
Theeraporn Puntheeranurak
Mobeen Raja
Azad Kumar
Barbara Wimmer
Isabel Neundlinger
Hermann Gruber
Peter Hinterdorfer
Rolf K.H. Kinne
Max Planck Institut fur molekulare Physiologie
Johannes Kepler Universitat Linz
Howard Hughes Medical Institute
Mahidol University
University of Alberta
National Institute on Aging
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2011
Citation: Biochimica et Biophysica Acta - Biomembranes. Vol.1808, No.1 (2011), 1-18
Abstract: Proteins mediating the transport of solutes across the cell membrane control the intracellular conditions in which life can occur. Because of the particular arrangement of spanning a lipid bilayer and the many conformations required for their function, transp ort proteins pose significant obstacles for the investigation of their structure-function relation. Crystallographic studies, if available, define the transmembrane segments in a "frozen" state and do not provide information on the dynamics of the extramembranous loops, which are similarly evolutionary conserved and thus as functionally important as the other parts of the protein. The current review presents biophysical methods that can shed light on the dynamics of transporters in the membrane. The techniques that are presented in some detail are single-molecule recognition atomic force microscopy and tryptophan scanning, which can report on the positioning of the loops and on conformational changes at the outer surface. Studies on a variety of symporters are discussed, which use gradients of sodium or protons as energy source to translocate (mainly organic) solutes against their concentration gradients into or out of the cells. Primarily, investigations of the sodium-glucose cotransporter SGLT1 are used as examples for this biophysical approach to understand transporter function. © 2010 Elsevier B.V. All rights reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=78649792808&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/11637
ISSN: 00052736
Appears in Collections:Scopus 2011-2015

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