| http://purl.uniprot.org/citations/11258890 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11258890 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11258890 | http://www.w3.org/2000/01/rdf-schema#comment | "The envelope glycoprotein of HIV-1 consists of the surface subunit gp120 and the transmembrane subunit gp41. Binding of gp120 to target cell receptors induces a conformational change in gp41, which then mediates the fusion of viral and cellular membranes. A buried isoleucine (Ile573) in a central trimeric coiled coil within the fusion-active gp41 ectodomain core is thought to favor this conformational activation. The role of Ile573 in determining the structure and function of the gp120-gp41 complex was investigated by mutating this residue to threonine, a nonconservative substitution in HIV-1 that occurs naturally in SIV. While the introduction of Thr573 markedly destabilized the gp41 core, the three-dimensional structure of the mutant trimer of hairpins was very similar to that of the wild-type molecule. A new hydrogen-bonding interaction between the buried Thr573 and Thr569 residues appears to allow formation of the trimer-of-hairpins structure at physiological temperature. The mutant envelope glycoprotein expressed in 293T cells and incorporated within pseudotyped virions displayed only a moderate reduction in syncytium-inducing capacity and virus infectivity, respectively. Our results demonstrate that the proper folding of the gp41 core underlies the membrane fusion properties of the gp120-gp41 complex. An understanding of the gp41 activation process may suggest novel strategies for vaccine and antiviral drug development."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0024759"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0024759"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Lu M."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Lu M."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Shu W."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Shu W."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Nunberg J.H."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Nunberg J.H."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Fagan M.B."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/author | "Fagan M.B."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/pages | "2797-2807"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/pages | "2797-2807"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/title | "Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: implications for membrane fusion."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/title | "Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: implications for membrane fusion."xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/volume | "40"xsd:string |
| http://purl.uniprot.org/citations/11258890 | http://purl.uniprot.org/core/volume | "40"xsd:string |