LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 1 of total 1

Search options

Article ; Online: Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism.

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

Proteins

2007  Volume 70, Issue 4, Page(s) 1488–1497

Abstract: ... peptide, recordings for Vpu(1-32)-S24L do not exhibit any noticeable channel activity. Recordings of WT ... Vpu from HIV-1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic ... Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like ...

Abstract 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 (Vpu(1-32)-W23L, Vpu(1-32)-R31V, Vpu(1-32)-S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu(1-32)-W23L has a considerable flickering pattern in the recordings and longer open times than Vpu(1-32). Whilst recordings for Vpu(1-32)-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 Vpu(1-32)-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.
MeSH term(s) Human Immunodeficiency Virus Proteins/chemistry ; Human Immunodeficiency Virus Proteins/genetics ; Human Immunodeficiency Virus Proteins/physiology ; Humans ; Ion Channels ; Kinetics ; Lipid Bilayers/metabolism ; Osmolar Concentration ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Viral Regulatory and Accessory Proteins/chemistry ; Viral Regulatory and Accessory Proteins/genetics ; Viral Regulatory and Accessory Proteins/physiology
Chemical Substances Human Immunodeficiency Virus Proteins ; Ion Channels ; Lipid Bilayers ; Peptide Fragments ; Viral Regulatory and Accessory Proteins ; vpu protein, Human immunodeficiency virus 1
Keywords covid19
Language English
Publishing date 2007-10-02
Publishing country United States
Document type Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID 806683-8
ISSN 1097-0134 ; 0887-3585
ISSN (online) 1097-0134
ISSN 0887-3585
DOI 10.1002/prot.21642
Shelf mark
Zs.A 2291: Show issues Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)
Database MEDical Literature Analysis and Retrieval System OnLINE

More links

Kategorien

To top