ArticleProtein science : a publication of the Protein Society1997
The extracellular domain of immunodeficiency virus gp41 protein: expression in Escherichia coli, purification, and crystallization.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS.FEBS letters · 2018Article
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- Overview of the purification of recombinant proteins.Current protocols in protein science · 2015Review
- Design and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery.Protein engineering, design & selection : PEDS · 2015Article
- Article
- HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.Structure (London, England : 1993) · 2014Article
- Preparation and extraction of insoluble (inclusion-body) proteins from Escherichia coli.Current protocols in protein science · 2012Article
- HIV envelope: challenges and opportunities for development of entry inhibitors.Trends in microbiology · 2011Review
- Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly.Journal of virology · 2010Article
- Transcytosis-blocking abs elicited by an oligomeric immunogen based on the membrane proximal region of HIV-1 gp41 target non-neutralizing epitopes.Current HIV research · 2008Article
- Peptide mimic of the HIV envelope gp120-gp41 interface.Journal of molecular biology · 2008Article
- In vitro screening for molecules that affect virus capsid assembly (and other protein association reactions).Nature protocols · 2007Article
- Preparation and extraction of insoluble (inclusion-body) proteins from Escherichia coli.Current protocols in protein science · 2004Article
- Sedimentation velocity studies of the high-molecular weight aggregates of the HIV gp41 ectodomain.Protein science : a publication of the Protein Society · 2004Article
- Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus type 1 gp140 envelope glycoprotein.Journal of virology · 2002Article
- Peptides corresponding to the heptad repeat motifs in the transmembrane protein (gp41) of human immunodeficiency virus type 1 elicit antibodies to receptor-activated conformations of the envelope glycoprotein.Journal of virology · 2001Article
- The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil.Journal of virology · 2000Article
- Monomer-trimer equilibrium of the ectodomain of SIV gp41: insight into the mechanism of peptide inhibition of HIV infection.Protein science : a publication of the Protein Society · 1999Article
- Is human thioredoxin monomeric or dimeric?Protein science : a publication of the Protein Society · 1999Article
- Rate and severity of HIV-associated dementia (HAD): correlations with Gp41 and iNOS.Molecular medicine (Cambridge, Mass.) · 1999Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The env gene of SIV and HIV-1 encodes a single glycoprotein gp 160, which is processed to give a noncovalent complex of the soluble glycoprotein gp120 and the transmembrane glycoprotein gp41. The extracellular region (ectodomain), minus the N-terminal fusion peptide, of gp41 from HIV-1 (residues 27-154) and SIV (residues 27-149) have been expressed in Escherichia coli. These insoluble proteins were solubilized and subjected to a simple purification and folding scheme, which results in high yields of soluble protein. Purified proteins have a trimeric subunit composition and high alpha-helical content, consistent with the predicted coil-coil structure. SIV gp41 containing a double cysteine mutation was crystallized. The crystals are suitable for X-ray structure determination and, preliminary analysis, together with additional biochemical evidence, indicates that the gp41 trimer is arranged as a parallel bundle with threefold symmetry.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.