This title appears in the Scientific Report :
2006
Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy
Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy
Based on structures made available by solution NMR, molecular models of the protein Vpu from HIV-1 were built and refined by 6 ns MD simulations in a fully hydrated lipid bilayer. Vpu is an 81 amino acid type I integral membrane protein encoded by the human immunodeficiency virus type-1 (HIV- 1) and...
Saved in:
Personal Name(s): | Lemaitre, V. |
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Wray, V. / Willbold, D. / Watts, A. / Fischer, W. B. | |
Contributing Institute: |
Biologische Strukturforschung; IBI-2 Jülich-Aachen Research Alliance - Simulation Sciences; JARA-SIM |
Published in: | Journal of biomolecular structure & dynamics, 23 (2006) S. 485 - 496 |
Imprint: |
Guilderland, NY
Adenine Press
2006
|
Physical Description: |
485 - 496 |
Document Type: |
Journal Article |
Research Program: |
Funktion und Dysfunktion des Nervensystems |
Series Title: |
Journal of Biomolecular Structure & Dynamics
23 |
Subject (ZB): | |
Publikationsportal JuSER |
Based on structures made available by solution NMR, molecular models of the protein Vpu from HIV-1 were built and refined by 6 ns MD simulations in a fully hydrated lipid bilayer. Vpu is an 81 amino acid type I integral membrane protein encoded by the human immunodeficiency virus type-1 (HIV- 1) and closely related simian immunodeficiency viruses (SIVs). Its role is to amplify viral release. Upon phosphorylation, the cytoplasmic domain adopts a more compact shape with helices 2 and 3 becoming almost parallel to each other. A loss of helicity for several residues belonging to the helices adjacent to both ends of the loop region containing serines 53 and 57 is observed. A fourth helix, present in one of: the NMR-based Structures of the cytoplasmic domain and located near the C-terminus, is lost upon phosphorylation. |