1szt
From Proteopedia
(New page: 200px<br /> <applet load="1szt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1szt, resolution 2.4Å" /> '''ATOMIC STRUCTURE OF ...) |
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| - | [[Image:1szt.gif|left|200px]]<br /> | + | [[Image:1szt.gif|left|200px]]<br /><applet load="1szt" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1szt, resolution 2.4Å" /> | caption="1szt, resolution 2.4Å" /> | ||
'''ATOMIC STRUCTURE OF A THERMOSTABLE SUBDOMAIN OF HIV-1 GP41'''<br /> | '''ATOMIC STRUCTURE OF A THERMOSTABLE SUBDOMAIN OF HIV-1 GP41'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Infection by HIV-1 involves the fusion of viral and cellular membranes | + | Infection by HIV-1 involves the fusion of viral and cellular membranes with subsequent transfer of viral genetic material into the cell. The HIV-1 envelope glycoprotein that mediates fusion consists of the surface subunit gp120 and the transmembrane subunit gp41. gp120 directs virion attachment to the cell-surface receptors, and gp41 then promotes viral-cell membrane fusion. A soluble, alpha-helical, trimeric complex within gp41 composed of N-terminal and C-terminal extraviral segments has been proposed to represent the core of the fusion-active conformation of the HIV-1 envelope. A thermostable subdomain denoted N34(L6)C28 can be formed by the N-34 and C-28 peptides connected by a flexible linker in place of the disulfide-bonded loop region. Three-dimensional structure of N34(L6)C28 reveals that three molecules fold into a six-stranded helical bundle. Three N-terminal helices within the bundle form a central, parallel, trimeric coiled coil, whereas three C-terminal helices pack in the reverse direction into three hydrophobic grooves on the surface of the N-terminal trimer. This thermostable subdomain displays the salient features of the core structure of the isolated gp41 subunit and thus provides a possible target for therapeutics designed selectively to block HIV-1 entry. |
==About this Structure== | ==About this Structure== | ||
| - | 1SZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http:// | + | 1SZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SZT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
[[Category: Tan, K.]] | [[Category: Tan, K.]] | ||
| - | [[Category: Wang, J | + | [[Category: Wang, J H.]] |
[[Category: coat protein]] | [[Category: coat protein]] | ||
[[Category: hiv-1 envelope glycoprotein]] | [[Category: hiv-1 envelope glycoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:02 2008'' |
Revision as of 13:08, 21 February 2008
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ATOMIC STRUCTURE OF A THERMOSTABLE SUBDOMAIN OF HIV-1 GP41
Overview
Infection by HIV-1 involves the fusion of viral and cellular membranes with subsequent transfer of viral genetic material into the cell. The HIV-1 envelope glycoprotein that mediates fusion consists of the surface subunit gp120 and the transmembrane subunit gp41. gp120 directs virion attachment to the cell-surface receptors, and gp41 then promotes viral-cell membrane fusion. A soluble, alpha-helical, trimeric complex within gp41 composed of N-terminal and C-terminal extraviral segments has been proposed to represent the core of the fusion-active conformation of the HIV-1 envelope. A thermostable subdomain denoted N34(L6)C28 can be formed by the N-34 and C-28 peptides connected by a flexible linker in place of the disulfide-bonded loop region. Three-dimensional structure of N34(L6)C28 reveals that three molecules fold into a six-stranded helical bundle. Three N-terminal helices within the bundle form a central, parallel, trimeric coiled coil, whereas three C-terminal helices pack in the reverse direction into three hydrophobic grooves on the surface of the N-terminal trimer. This thermostable subdomain displays the salient features of the core structure of the isolated gp41 subunit and thus provides a possible target for therapeutics designed selectively to block HIV-1 entry.
About this Structure
1SZT is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Atomic structure of a thermostable subdomain of HIV-1 gp41., Tan K, Liu J, Wang J, Shen S, Lu M, Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12303-8. PMID:9356444
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