2005
DOI: 10.1016/j.jmb.2005.05.030
|View full text |Cite
|
Sign up to set email alerts
|

The HIV Fusion Peptide Adopts Intermolecular Parallel β-Sheet Structure in Membranes when Stabilized by the Adjacent N-Terminal Heptad Repeat: A 13C FTIR Study

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

4
64
1

Year Published

2006
2006
2013
2013

Publication Types

Select...
6
1

Relationship

2
5

Authors

Journals

citations
Cited by 46 publications
(70 citation statements)
references
References 87 publications
4
64
1
Order By: Relevance
“…However, IR data on constructs which contain the first 34 or 70 residues of gp41 support an in-register parallel strand arrangement (44). These latter constructs contain the 23-residues of HFPmn as well as an additional 11 or 47 C-terminal residues.…”
Section: Strand Arrangementmentioning
confidence: 92%
See 1 more Smart Citation
“…However, IR data on constructs which contain the first 34 or 70 residues of gp41 support an in-register parallel strand arrangement (44). These latter constructs contain the 23-residues of HFPmn as well as an additional 11 or 47 C-terminal residues.…”
Section: Strand Arrangementmentioning
confidence: 92%
“…Models for the helical structure have been developed based on nuclear magnetic resonance (NMR), electron spin resonance (ESR), infrared (IR), and circular dichroism (CD) data, as well as computer simulations (33)(34)(35)(36)(37)(38)(39). A β hairpin model for non-helical structure has been proposed based on IR and surface activity measurements in membranes (40).Fluorescence, ESR, IR, and solid-state NMR data also suggest that the nonhelical HFPs in membranes form oligomeric structures (10,(41)(42)(43)(44). These oligomeric structures may be important as evidenced by envelope protein trimerization and by experiments and modeling which indicate that the fusion site contains multiple trimers and a corresponding high HFP concentration (17,18,45).…”
mentioning
confidence: 99%
“…So far, structural information for many fusion peptides has been revealed by a variety of spectroscopic and computational methods. The HIV gp41 fusion peptide was shown to form an ␣-helix in membrane-mimicking environments (23,30,42). The three-dimensional structure of the Ebola fusion peptide displays a 3 10 -helix in the central part of the molecule (13).…”
Section: Discussionmentioning
confidence: 99%
“…The three-dimensional structure of the fusion peptide is essential to understanding this mechanism. Some of the structures of fusion peptides of different viruses, such as the fusion peptide of influenza virus hemagglutinin (HA) (16,28) and the fusion peptide of HIV gp41 (7,23,30,42), have been determined by nuclear magnetic resonance (NMR) and other techniques.…”
mentioning
confidence: 99%
“…As it has been proposed for the HIV fusion peptide, hydrophobic monomers of H5WYG could self-assemble into a parallel β-sheet configuration. [19] Indeed, there are possibilities for inter-peptide π -stacking of aromatic side-chains of the two phenylalanines in positions 3 and 10 as well as of the two tryptophans in positions 14 and 21. Moreover, uncharged imidazole groups of histidine residues in positions 4, 8, 11, 15 and 19 can also form π -stacking.…”
Section: H15amentioning
confidence: 99%