1phv

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{{Theoretical_model}}
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[[Image:1phv.png|left|200px]]
 
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==COMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV- 1 AND HIV-2 PROTEASES==
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The line below this paragraph, containing "STRUCTURE_1phv", creates the "Structure Box" on the page.
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<StructureSection load='1phv' size='340' side='right'caption='[[1phv]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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</table>
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{{STRUCTURE_1phv| PDB=1phv | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===COMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV- 1 AND HIV-2 PROTEASES===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_1946342}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1phv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 1946342 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_1946342}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHV OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:1946342</ref><references group="xtra"/>
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[[Category: Gustchina, A]]
[[Category: Gustchina, A]]
[[Category: Weber, I T]]
[[Category: Weber, I T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:17:46 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

COMPARATIVE ANALYSIS OF THE SEQUENCES AND STRUCTURES OF HIV- 1 AND HIV-2 PROTEASES

PDB ID 1phv

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