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rdf:type |
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lifeskim:mentions |
umls-concept:C0019691,
umls-concept:C0019704,
umls-concept:C0030956,
umls-concept:C0332197,
umls-concept:C0332466,
umls-concept:C0376315,
umls-concept:C0599219,
umls-concept:C0913822,
umls-concept:C0913823,
umls-concept:C1711351,
umls-concept:C1749467
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pubmed:issue |
7
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pubmed:dateCreated |
1996-6-6
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pubmed:abstractText |
The human immunodeficiency virus-1 (HIV-1) envelope glycoprotein is composed of a soluble glycopolypeptide gp120 and a transmembrane glycopolypeptide gp41. These subunits form non-covalently linked oligomers on the surface of infected cells, virions and cells transfected with the complete env gene. Two length variants of the extracellular domain of gp41 (aa 21-166 and aa 39-166), that both lack the N-terminal fusion peptide and the C-terminal membrane anchor and cytoplasmic domain, have been expressed in insect cells to yield soluble oligomeric gp41 proteins. Oligomerization was confirmed by chemical cross-linking and gel filtration. Electron microscopy and circular dichroism measurements indicate a rod-like molecule with a high alpha-helical content and a high melting temperature (78 degrees C). The binding of monoclonal antibody Fab fragments dramatically increased the solubility of both gp41 constructs. We propose that gp41 folds into its membrane fusion-active conformation, when expressed alone.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-1438243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-1537337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-1713252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-1714520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-1871974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-1995942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-201090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-217151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2177097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2214033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2238472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2300552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2410792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2541505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2672564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2786089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2788443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2986290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-2994223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-3094962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-3183628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-3629244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-3643678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-6083454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-6096719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-6864784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-6951181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-7512157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-7538176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-7707497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-7809100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-7937889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-8072525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-8500173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8612573-8618870
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1507-14
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8612573-Animals,
pubmed-meshheading:8612573-Antibodies, Monoclonal,
pubmed-meshheading:8612573-Cell Line,
pubmed-meshheading:8612573-Disulfides,
pubmed-meshheading:8612573-Genes, env,
pubmed-meshheading:8612573-HIV Antibodies,
pubmed-meshheading:8612573-HIV Envelope Protein gp120,
pubmed-meshheading:8612573-HIV Envelope Protein gp41,
pubmed-meshheading:8612573-HIV-1,
pubmed-meshheading:8612573-Humans,
pubmed-meshheading:8612573-Immunoglobulin Fab Fragments,
pubmed-meshheading:8612573-Insects,
pubmed-meshheading:8612573-Microscopy, Electron,
pubmed-meshheading:8612573-Protein Conformation,
pubmed-meshheading:8612573-Protein Structure, Secondary,
pubmed-meshheading:8612573-Solubility,
pubmed-meshheading:8612573-Thermodynamics,
pubmed-meshheading:8612573-Viral Fusion Proteins
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pubmed:year |
1996
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pubmed:articleTitle |
The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide.
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