Structural implications of mutations assessed by molecular dynamics: Vpu1-32 from HIV-1

J. Krüger; Wolfgang B. Fischer

doi:10.1007/s00249-009-0487-0

Structural implications of mutations assessed by molecular dynamics: Vpu_1-32 from HIV-1

J. Krüger, Wolfgang B. Fischer

Institute of Biophotonics

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Structural pore models are generated for Vpu_1-32WT from HIV-1 as well as for three mutants W23L, S24L and R31V. A computational methodology is employed which samples the whole conformational space of the pentameric assemblies of Vpu. The analysis of the related energy landscape reveals a small set of reasonable pore models, which are thoroughly investigated regarding their structural properties as well as their putative stability under native-like conditions. The models are also discussed in respect of earlier experimental Wndings about their channel activities. The study proposes functional pores reXecting the experimentally found conductance states of Vpu and its mutants.

Original language	English
Pages (from-to)	1069-1077
Number of pages	9
Journal	European Biophysics Journal
Volume	39
Issue number	7
DOIs	https://doi.org/10.1007/s00249-009-0487-0
State	Published - Jun 2010

Keywords

Conductance
HIV-1
Membrane protein
Mutation
Protein assembly
Vpu

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1007/s00249-009-0487-0

Cite this

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title = "Structural implications of mutations assessed by molecular dynamics: Vpu1-32 from HIV-1",

abstract = "Structural pore models are generated for Vpu1-32WT from HIV-1 as well as for three mutants W23L, S24L and R31V. A computational methodology is employed which samples the whole conformational space of the pentameric assemblies of Vpu. The analysis of the related energy landscape reveals a small set of reasonable pore models, which are thoroughly investigated regarding their structural properties as well as their putative stability under native-like conditions. The models are also discussed in respect of earlier experimental Wndings about their channel activities. The study proposes functional pores reXecting the experimentally found conductance states of Vpu and its mutants.",

keywords = "Conductance, HIV-1, Membrane protein, Mutation, Protein assembly, Vpu",

author = "J. Kr{\"u}ger and Fischer, {Wolfgang B.}",

note = "Funding Information: Acknowledgment WBF acknowledges National Yang-Ming University and the government of Taiwan for Wnancial support (Aim of Excellence Program), as well as the National Science Council of Taiwan (NSC). J.K. acknowledges a fellowship granted jointly by the Alexander von Humboldt-Foundation and NSC. We thank the Paderborn Center for Parallel Computing PC2 (http://wwwcs.uni-paderborn.de/pc2/) for providing computer time.",

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AB - Structural pore models are generated for Vpu1-32WT from HIV-1 as well as for three mutants W23L, S24L and R31V. A computational methodology is employed which samples the whole conformational space of the pentameric assemblies of Vpu. The analysis of the related energy landscape reveals a small set of reasonable pore models, which are thoroughly investigated regarding their structural properties as well as their putative stability under native-like conditions. The models are also discussed in respect of earlier experimental Wndings about their channel activities. The study proposes functional pores reXecting the experimentally found conductance states of Vpu and its mutants.

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