3phv
From Proteopedia
(New page: 200px<br /> <applet load="3phv" size="450" color="white" frame="true" align="right" spinBox="true" caption="3phv, resolution 2.7Å" /> '''X-RAY ANALYSIS OF HI...) |
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| - | [[Image:3phv.gif|left|200px]]<br /> | + | [[Image:3phv.gif|left|200px]]<br /><applet load="3phv" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="3phv" size=" | + | |
caption="3phv, resolution 2.7Å" /> | caption="3phv, resolution 2.7Å" /> | ||
'''X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES'''<br /> | '''X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Knowledge of the tertiary structure of the proteinase from human | + | Knowledge of the tertiary structure of the proteinase from human immunodeficiency virus HIV-1 is important to the design of inhibitors that might possess antiviral activity and thus be useful in the treatment of AIDS. The conserved Asp-Thr/Ser-Gly sequence in retroviral proteinases suggests that they exist as dimers similar to the ancestor proposed for the pepsins. Although this has been confirmed by X-ray analyses of Rous sarcoma virus and HIV-1 proteinases, these structures have overall folds that are similar to each other only where they are also similar to the pepsins. We now report a further X-ray analysis of a recombinant HIV-1 proteinase at 2.7 A resolution. The polypeptide chain adopts a fold in which the N- and C-terminal strands are organized together in a four-stranded beta-sheet. A helix precedes the single C-terminal strand, as in the Rous sarcoma virus proteinase and also in a synthetic HIV-1 proteinase, in which the cysteines have been replaced by alpha-aminobuytric acid. The structure reported here provides an explanation for the amino acid invariance amongst retroviral proteinases, but differs from that reported earlier in some residues that are candidates for substrate interactions at P3, and in the mode of intramolecular cleavage during processing of the polyprotein. |
==About this Structure== | ==About this Structure== | ||
| - | 3PHV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_hxb2) Human immunodeficiency virus type 1 (isolate hxb2)]. Full crystallographic information is available from [http:// | + | 3PHV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_hxb2) Human immunodeficiency virus type 1 (isolate hxb2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHV OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Human immunodeficiency virus type 1 (isolate hxb2)]] | [[Category: Human immunodeficiency virus type 1 (isolate hxb2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L.]] |
| - | [[Category: Danley, D | + | [[Category: Danley, D E.]] |
| - | [[Category: Geoghegan, K | + | [[Category: Geoghegan, K F.]] |
| - | [[Category: Hawrylik, S | + | [[Category: Hawrylik, S J.]] |
[[Category: Hemmings, A.]] | [[Category: Hemmings, A.]] | ||
| - | [[Category: Hobart, P | + | [[Category: Hobart, P M.]] |
[[Category: Lapatto, R.]] | [[Category: Lapatto, R.]] | ||
[[Category: Wilderspin, A.]] | [[Category: Wilderspin, A.]] | ||
| - | [[Category: Wood, S | + | [[Category: Wood, S P.]] |
[[Category: hydrolase(aspartic proteinase)]] | [[Category: hydrolase(aspartic proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:54 2008'' |
Revision as of 17:10, 21 February 2008
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X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES
Overview
Knowledge of the tertiary structure of the proteinase from human immunodeficiency virus HIV-1 is important to the design of inhibitors that might possess antiviral activity and thus be useful in the treatment of AIDS. The conserved Asp-Thr/Ser-Gly sequence in retroviral proteinases suggests that they exist as dimers similar to the ancestor proposed for the pepsins. Although this has been confirmed by X-ray analyses of Rous sarcoma virus and HIV-1 proteinases, these structures have overall folds that are similar to each other only where they are also similar to the pepsins. We now report a further X-ray analysis of a recombinant HIV-1 proteinase at 2.7 A resolution. The polypeptide chain adopts a fold in which the N- and C-terminal strands are organized together in a four-stranded beta-sheet. A helix precedes the single C-terminal strand, as in the Rous sarcoma virus proteinase and also in a synthetic HIV-1 proteinase, in which the cysteines have been replaced by alpha-aminobuytric acid. The structure reported here provides an explanation for the amino acid invariance amongst retroviral proteinases, but differs from that reported earlier in some residues that are candidates for substrate interactions at P3, and in the mode of intramolecular cleavage during processing of the polyprotein.
About this Structure
3PHV is a Single protein structure of sequence from Human immunodeficiency virus type 1 (isolate hxb2). Full crystallographic information is available from OCA.
Reference
X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes., Lapatto R, Blundell T, Hemmings A, Overington J, Wilderspin A, Wood S, Merson JR, Whittle PJ, Danley DE, Geoghegan KF, et al., Nature. 1989 Nov 16;342(6247):299-302. PMID:2682266
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