NDLI: HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.

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HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lakomek, Nils-Alexander Kaufman, Joshua D. Stahl, Stephen J. Wingfield, Paul T.
Description	Author Affiliation: Lakomek NA ( Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD 20892-0520, USA. Electronic address: nall@nmr.mpibpc.mpg.de.); Kaufman JD ( Protein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892-2775, USA.); Stahl SJ ( Protein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892-2775, USA.); Wingfield PT ( Protein Expression Laboratory, NIAMS, National Institutes of Health, Bethesda, MD 20892-2775, USA. Electronic address: wingfiep@mail.nih.gov.)
Abstract	Human immunodeficiency viral (HIV-1) fusion is mediated by the viral envelope gp120/gp41 complex (ENVelope glycoprotein). After gp120 shedding, gp41 is exposed and elicits membrane fusion via a cascade of conformational changes. In contrast to prefusion and postfusion conformation, little is known about any intermediate conformation. We report on a solution NMR investigation of homotrimeric HIV-1 gp41(27-194), comprising the transmembrane region and reconstituted in dodecyl phosphocholine (DPC) micelles. The protein is mainly -helical, but experiences internal dynamics on the nanosecond and micro to millisecond time scale and transient -helical behavior for certain residues in the N-terminal heptad repeat (NHR). Strong lipid interactions are observed, in particular for C-terminal residues of the NHR and imunodominant loop region connecting NHR and C-terminal heptad repeat (CHR). Our data indicate an extended conformation with features anticipated for a prefusion intermediate, presumably in exchange with a lowly populated postfusion six-helical bundle conformation.
File Format	HTM / HTML
ISSN	09692126
e-ISSN	18784186
DOI	10.1016/j.str.2014.06.016
Journal	Structure
Issue Number	9
Volume Number	22
Language	English
Publisher	Elsevier
Publisher Date	2014-09-02
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Hiv Envelope Protein Gp41 Chemistry Phosphorylcholine Analogs & Derivatives Detergents Hiv-1 Micelles Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Structure, Quaternary Protein Structure, Secondary Virus Internalization Research Support, N.i.h., Intramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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HIV-1 viral envelope protein gp41: An NMR investigation of dodecyl phosphocholine embedded gp41 reveals a dynamic pre-fusion intermediate conformation

Capturing glimpses of an elusive HIV gp41 prehairpin fusion intermediate.

Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion.

Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion.

NMR structural studies of the Ste11 SAM domain in the dodecyl phosphocholine micelle.

Structure and immunogenicity of a peptide vaccine, including the complete HIV-1 gp41 2F5 epitope: implications for antibody recognition mechanism and immunogen design.

Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy.

Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles.

Designing a soluble near full-length HIV-1 gp41 trimer.

HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.

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Designing a soluble near full-length HIV-1 gp41 trimer.

HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.