1hhp
From Proteopedia
(New page: 200px<br /> <applet load="1hhp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hhp, resolution 2.7Å" /> '''THE THREE-DIMENSIONA...) |
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| - | [[Image:1hhp.gif|left|200px]]<br /> | + | [[Image:1hhp.gif|left|200px]]<br /><applet load="1hhp" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hhp" size=" | + | |
caption="1hhp, resolution 2.7Å" /> | caption="1hhp, resolution 2.7Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE HIV-1 ISOLATE BRU'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE HIV-1 ISOLATE BRU'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the aspartyl protease encoded by the gene pol of | + | The crystal structure of the aspartyl protease encoded by the gene pol of the human immunodeficiency virus (HIV-1, isolate BRU) has been determined to 2.7 A resolution. The enzyme, expressed as an insoluble denatured polypeptide in inclusion bodies of Escherichia coli has been renatured and crystallized. It differs by several amino acid replacements from the homologous enzymes of other HIV-1 isolates. A superposition of the C alpha-backbone of the BRU protease with that of the SF2 protease gives a roots mean square positional difference of 0.45 A. Thus, neither the denaturation/renaturation process nor the amino acid replacements have a noticeable effect on the three-dimensional structure of the BRU protease or on the detailed conformation of the catalytic site, which is very similar to that of other aspartyl proteases. |
==About this Structure== | ==About this Structure== | ||
| - | 1HHP 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_bru) Human immunodeficiency virus type 1 (isolate bru)]. Full crystallographic information is available from [http:// | + | 1HHP 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_bru) Human immunodeficiency virus type 1 (isolate bru)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human immunodeficiency virus type 1 (isolate bru)]] | [[Category: Human immunodeficiency virus type 1 (isolate bru)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alzari, P | + | [[Category: Alzari, P M.]] |
[[Category: Spinelli, S.]] | [[Category: Spinelli, S.]] | ||
[[Category: hydrolase(acid proteinase)]] | [[Category: hydrolase(acid proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:26 2008'' |
Revision as of 11:01, 21 February 2008
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THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE HIV-1 ISOLATE BRU
Overview
The crystal structure of the aspartyl protease encoded by the gene pol of the human immunodeficiency virus (HIV-1, isolate BRU) has been determined to 2.7 A resolution. The enzyme, expressed as an insoluble denatured polypeptide in inclusion bodies of Escherichia coli has been renatured and crystallized. It differs by several amino acid replacements from the homologous enzymes of other HIV-1 isolates. A superposition of the C alpha-backbone of the BRU protease with that of the SF2 protease gives a roots mean square positional difference of 0.45 A. Thus, neither the denaturation/renaturation process nor the amino acid replacements have a noticeable effect on the three-dimensional structure of the BRU protease or on the detailed conformation of the catalytic site, which is very similar to that of other aspartyl proteases.
About this Structure
1HHP is a Single protein structure of sequence from Human immunodeficiency virus type 1 (isolate bru). Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU., Spinelli S, Liu QZ, Alzari PM, Hirel PH, Poljak RJ, Biochimie. 1991 Nov;73(11):1391-6. PMID:1799632
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