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Basic Characteristics of Mutations
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Mutation Site
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S24L |
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Mutation Site Sentence
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Peptides corresponding to the TM domain of Vpu (Vpu1-32) and mutant peptides (Vpu1-32-W23L, Vpu1-32-R31V, Vpu1-32-S24L) have been synthesized and reconstituted into artificial lipid bilayers. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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Vpu |
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Standardized Encoding Gene
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Vpu
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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-
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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17910056
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Title
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Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism
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Author
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Mehnert T,Routh A,Judge PJ,Lam YH,Fischer D,Watts A,Fischer WB
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Journal
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Proteins
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Journal Info
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2008 Mar;70(4):1488-97
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Abstract
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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.
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Sequence Data
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-
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