Normally, the author and publisher would be credited here. This content was accessible as of December 29, 2012, and it was downloaded then by Andy Schmitz in an effort to preserve the availability of this book. See the license for more details, but that basically means you can share this book as long as you credit the author (but see below), don't make money from it, and do make it available to everyone else under the same terms. Structural comparison of the uniporter GLUT1 with its bacterial homologue XylE, a proton-coupled xylose symporter, allows examination of the transport mechanisms of both passive facilitators and active transporters.ġ] State Key Laboratory of Bio-membrane and Membrane Biotechnology, Tsinghua University, Beijing 100084, China Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, China.This book is licensed under a Creative Commons by-nc-sa 3.0 license. Structure-based analysis of these mutations provides an insight into the alternating access mechanism of GLUT1 and other members of the sugar porter subfamily.
This structure allows accurate mapping and potential mechanistic interpretation of disease-associated mutations in GLUT1. The full-length protein, which has a canonical major facilitator superfamily fold, is captured in an inward-open conformation. Here we report the crystal structure of human GLUT1 at 3.2 Å resolution. Despite decades of investigation, the structure of GLUT1 remains unknown. Dysfunctional mutations may lead to GLUT1 deficiency syndrome, whereas overexpression of GLUT1 is a prognostic indicator for cancer. The glucose transporter GLUT1 catalyses facilitative diffusion of glucose into erythrocytes and is responsible for glucose supply to the brain and other organs.
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