Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism

T. Mehnert, A. Routh, P. J. Judge, Y. H. Lam, D. Fischer, A. Watts, W. B. Fischer*

*此作品的通信作者

研究成果: Article同行評審

55 引文 斯高帕斯(Scopus)

摘要

Vpu from HIV-1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu 1-32) and mutant peptides (Vpu1-32-W23L, Vpu 1-32-R31V, Vpu1-32-S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu1-32-W23L has a considerable flickering pattern in the recordings and longer open times than Vpu1-32. Whilst recordings for Vpu1-32-R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu 1-32-S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu1-32-W23L indicate Michaelis-Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics.

原文English
頁(從 - 到)1488-1497
頁數10
期刊Proteins: Structure, Function and Genetics
70
發行號4
DOIs
出版狀態Published - 3月 2008

指紋

深入研究「Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism」主題。共同形成了獨特的指紋。

引用此