Perturbation of Critical Prolines in Gloeobacter violaceus Ligand-gated Ion Channel (GLIC) Supports Conserved Gating Motions among Cys-loop Receptors
作者： Matthew Rienzo , Angela R. Rocchi , Stephanie D. Threatt , Dennis A. Dougherty , Sarah C. R. Lummis
关键词: Xenopus 、 Biophysics 、 Ligand-gated ion channel 、 Cys-loop receptors 、 Biology 、 Biochemistry 、 Ion channel 、 Peptide sequence 、 GLIC 、 Gating 、 Protein structure
摘要: Gloeobacter violaceus ligand-gated ion channel (GLIC) has served as a valuable structural and functional model for the eukaryotic Cys-loop receptor superfamily. In other receptors, we have previously demonstrated crucial roles played by several conserved prolines. Here explore role of prolines in gating transitions GLIC. As conventional substitutions at some positions resulted nonfunctional proteins, used vivo non-canonical amino acid mutagenesis to determine specific requirements these sites. Receptors were expressed heterologously Xenopus laevis oocytes, whole-cell electrophysiology was monitor activity. Pro-119 Cys-loop, Pro-198 Pro-203 M1 helix, Pro-299 M4 helix sensitive substitution, distinct activity revealed each. context available data GLIC, behaviors Pro-119, Pro-203, mutants are consistent with earlier proline work. However, site displays unique phenotype that gives evidence importance region surrounding this residue correct functioning
sci-hub.se 参考文章(36)
Mark W. Nowak, Justin P. Gallivan, Scott K. Silverman, Cesar G. Labarca, Dennis A. Dougherty, Henry A. Lester, In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system. Methods in Enzymology. ,vol. 293, pp. 504- 529 ,(1998) , 10.1016/S0076-6879(98)93031-2
Paul S. Miller, A. Radu Aricescu, Crystal structure of a human GABAA receptor Nature. ,vol. 512, pp. 270- 275 ,(2014) , 10.1038/NATURE13293
G. Gonzalez-Gutierrez, L. G. Cuello, S. K. Nair, C. Grosman, Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography Proceedings of the National Academy of Sciences of the United States of America. ,vol. 110, pp. 18716- 18721 ,(2013) , 10.1073/PNAS.1313156110
Camille M. Hénault, Jiayin Sun, J.P. Daniel Therien, Corrie J.B. daCosta, Casey L. Carswell, Jonathan M. Labriola, Peter F. Juranka, John E. Baenziger, The role of the M4 lipid-sensor in the folding, trafficking, and allosteric modulation of nicotinic acetylcholine receptors. Neuropharmacology. ,vol. 96, pp. 157- 168 ,(2015) , 10.1016/J.NEUROPHARM.2014.11.011
Ulf Reimer, Gerd Scherer, Mario Drewello, Susanne Kruber, Mike Schutkowski, Gunter Fischer, SIDE-CHAIN EFFECTS ON PEPTIDYL-PROLYL CIS/TRANS ISOMERISATION Journal of Molecular Biology. ,vol. 279, pp. 449- 460 ,(1998) , 10.1006/JMBI.1998.1770
Ethan B. Van Arnam, Henry A. Lester, Dennis A. Dougherty, Dissecting the functions of conserved prolines within transmembrane helices of the D2 dopamine receptor. ACS Chemical Biology. ,vol. 6, pp. 1063- 1068 ,(2011) , 10.1021/CB200153G
Matthew Rienzo, Sarah C.R. Lummis, Dennis A. Dougherty, Structural Requirements in the Transmembrane Domain of GLIC Revealed by Incorporation of Noncanonical Histidine Analogs Chemistry & Biology. ,vol. 21, pp. 1700- 1706 ,(2014) , 10.1016/J.CHEMBIOL.2014.10.019
Ricarda J. C. Hilf, Raimund Dutzler, Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel Nature. ,vol. 457, pp. 115- 118 ,(2009) , 10.1038/NATURE07461
L. Sauguet, A. Shahsavar, F. Poitevin, C. Huon, A. Menny, A. Nemecz, A. Haouz, J.-P. Changeux, P.-J. Corringer, M. Delarue, Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation Proceedings of the National Academy of Sciences of the United States of America. ,vol. 111, pp. 966- 971 ,(2014) , 10.1073/PNAS.1314997111
Ludovic Sauguet, Rebecca J. Howard, Laurie Malherbe, Ui S. Lee, Pierre-Jean Corringer, R. Adron Harris, Marc Delarue, Structural basis for potentiation by alcohols and anaesthetics in a ligand-gated ion channel Nature Communications. ,vol. 4, pp. 1697- 1697 ,(2013) , 10.1038/NCOMMS2682