Source:http://linkedlifedata.com/resource/pubmed/id/11921231
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2002-3-28
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pubmed:abstractText |
The selective proteolytic activation of the HIV-1 envelope glycoprotein gp160 by furin and other precursor convertases (PCs) occurs at the carboxyl side of the sequence Arg508-Glu-Lys-Arg511 (site 1), in spite of the presence of another consensus sequence: Lys500-Ala-Lys-Arg503 (site 2). We report on the solution structural analysis of a 19-residue synthetic peptide, p498, which spans the two gp160-processing sites 1 and 2, and is properly digested by furin at site 1. A molecular model is obtained for p498, by means of molecular dynamics simulations, from NMR data collected in trifluoroethanol/water. The peptide N-terminal side presents a 9-residue helical segment, enclosing the processing site 2; the C-terminal segment can be described as a loop exposing the processing site 1. A hypothesis for the docking of p498 onto the catalytic domain of human furin, modeled by homology and fitting previous site-directed mutagenesis studies, is also presented. p498 site 1 is shown to have easy access to the furin catalytic site, unlike the nonphysiological site 2. Finally, on the basis of available data, we suggest a possible structural motif required for the gp160-PCs recognition.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Furin,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp160,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0947-6539
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1467-73
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pubmed:dateRevised |
2009-8-4
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pubmed:meshHeading |
pubmed-meshheading:11921231-Amino Acid Sequence,
pubmed-meshheading:11921231-Catalytic Domain,
pubmed-meshheading:11921231-Consensus Sequence,
pubmed-meshheading:11921231-Furin,
pubmed-meshheading:11921231-HIV Envelope Protein gp160,
pubmed-meshheading:11921231-Humans,
pubmed-meshheading:11921231-Models, Molecular,
pubmed-meshheading:11921231-Peptide Fragments,
pubmed-meshheading:11921231-Protein Structure, Secondary,
pubmed-meshheading:11921231-Solutions,
pubmed-meshheading:11921231-Subtilisins
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pubmed:year |
2002
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pubmed:articleTitle |
Structural investigation of the HIV-1 envelope glycoprotein gp160 cleavage site.
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pubmed:affiliation |
Dipartimento di Chimica, Università di Napoli Federico II, Complesso Universitario Monte S. Angelo, via Cintia, 80126 Napoli, Italy.
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pubmed:publicationType |
Journal Article
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