Journal article
Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase
R Trenker, ME Call, MJ Call
Journal of the American Chemical Society | Published : 2015
DOI: 10.1021/jacs.5b11354
Abstract
The mechanisms of assembly and function for many important type I/II (single-pass) transmembrane (TM) receptors are proposed to involve the formation and/or alteration of specific interfaces among their membrane-embedded α-helical TM domains. The application of lipidic cubic phase (LCP) bilayer media for crystallization of single-α-helical TM complexes has the potential to provide valuable structural and mechanistic insights into many such systems. However, the fidelity of the interfaces observed in crowded crystalline arrays has been difficult to establish from the very limited number of such structures determined using X-ray diffraction data. Here we examine this issue using the glycophori..
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Awarded by Human Frontier Science Program
Funding Acknowledgements
We thank Kelly Rogers and Mark Scott at the WEHI Imaging Facility for assistance with FRAP analysis, Janet Newman for materials, Jacqui Gulbis for helpful advice on structure refinement, Steven O. Smith for provision of the ssNMR structure coordinates, and Cyrus Tan and Logesvaran Krshnan for helpful discussions. We acknowledge the use of the CSIRO Collaborative Crystallization Centre (C3) for LCP screening. Part of this research was carried out at the MX2 beamline of the Australian Synchrotron, and we thank the beamline scientists for their technical support. This work was supported by the Human Frontier Science Program (Grant RGP0064 to M.E.C.) and the National Health and Medical Research Council (Project Grant 1030902 to M.E.C. and M.J.C.; IRIISS Infrastructure Support to WEHI). M.E.C. is supported by ARC QEII Fellowship DP110104369. M.J.C. is supported by ARC Future Fellowship FT120100145.