1hhp
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(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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Revision as of 11:59, 8 November 2007
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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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