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| - | [[Image:1f23.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1f23.png|left|200px]] |
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| | {{STRUCTURE_1f23| PDB=1f23 | SCENE= }} | | {{STRUCTURE_1f23| PDB=1f23 | SCENE= }} |
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| - | '''CONTRIBUTION OF A BURIED HYDROGEN BOND TO HIV-1 ENVELOPE GLYCOPROTEIN STRUCTURE AND FUNCTION'''
| + | ===CONTRIBUTION OF A BURIED HYDROGEN BOND TO HIV-1 ENVELOPE GLYCOPROTEIN STRUCTURE AND FUNCTION=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11258890}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11258890 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11258890}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hiv-1 envelope protein]] | | [[Category: Hiv-1 envelope protein]] |
| | [[Category: Membrane fusion]] | | [[Category: Membrane fusion]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:47:43 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:21:35 2008'' |
Revision as of 23:21, 30 June 2008
Template:STRUCTURE 1f23
CONTRIBUTION OF A BURIED HYDROGEN BOND TO HIV-1 ENVELOPE GLYCOPROTEIN STRUCTURE AND FUNCTION
Template:ABSTRACT PUBMED 11258890
About this Structure
1F23 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: implications for membrane fusion., Liu J, Shu W, Fagan MB, Nunberg JH, Lu M, Biochemistry. 2001 Mar 6;40(9):2797-807. PMID:11258890
Page seeded by OCA on Tue Jul 1 02:21:35 2008
