1phv: Difference between revisions
New page: '''Theoretical Model''' The entry 1PHV is a Theoretical Model titled 'COMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV-1 AND HIV-2 PROTEASES'. Category:Theoretical Model ... |
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{{Theoretical_model}} | |||
==COMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV- 1 AND HIV-2 PROTEASES== | |||
<StructureSection load='1phv' size='340' side='right'caption='[[1phv]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PHV FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1phv FirstGlance], [https://www.ebi.ac.uk/pdbsum/1phv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1phv ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The different isolates available for HIV-1 and HIV-2 were compared for the region of the protease (PR) sequence, and the variations in amino acids were analyzed with respect to the crystal structure of HIV-1 PR with inhibitor. Based on the extensive homology (39 identical out of 99 residues), models were built of the HIV-2 PR complexed with two different aspartic protease inhibitors, acetylpepstatin and a renin inhibitor, H-261. Comparison of the HIV-1 PR crystal structure and the HIV-2 PR model structure and the analysis of the changes found in different isolates showed that correlated substitutions occur in the hydrophobic interior of the molecule and at surface residues involved in ionic or hydrogen bond interactions. The substrate binding residues of HIV-1 and HIV-2 PRs show conservative substitutions of four residues. The difference in affinity of HIV-1 and HIV-2 PRs for the two inhibitors appears to be due in part to the change of Val 32 in HIV-1 PR to Ile in HIV-2 PR. | |||
Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases.,Gustchina A, Weber IT Proteins. 1991;10(4):325-39. PMID:1946342<ref>PMID:1946342</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1phv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Gustchina, A]] | |||
[[Category: Weber, I T]] | |||
Latest revision as of 12:30, 8 September 2021
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COMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV- 1 AND HIV-2 PROTEASESCOMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV- 1 AND HIV-2 PROTEASES
Structural highlights
Publication Abstract from PubMedThe different isolates available for HIV-1 and HIV-2 were compared for the region of the protease (PR) sequence, and the variations in amino acids were analyzed with respect to the crystal structure of HIV-1 PR with inhibitor. Based on the extensive homology (39 identical out of 99 residues), models were built of the HIV-2 PR complexed with two different aspartic protease inhibitors, acetylpepstatin and a renin inhibitor, H-261. Comparison of the HIV-1 PR crystal structure and the HIV-2 PR model structure and the analysis of the changes found in different isolates showed that correlated substitutions occur in the hydrophobic interior of the molecule and at surface residues involved in ionic or hydrogen bond interactions. The substrate binding residues of HIV-1 and HIV-2 PRs show conservative substitutions of four residues. The difference in affinity of HIV-1 and HIV-2 PRs for the two inhibitors appears to be due in part to the change of Val 32 in HIV-1 PR to Ile in HIV-2 PR. Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases.,Gustchina A, Weber IT Proteins. 1991;10(4):325-39. PMID:1946342[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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