1hvp: Difference between revisions
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==MOLECULAR MODELING OF THE HIV-1 PROTEASE AND ITS SUBSTRATE BINDING SITE== | |||
<StructureSection load='1hvp' size='340' side='right' caption='[[1hvp]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HVP FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hvp FirstGlance], [http://www.ebi.ac.uk/pdbsum/1hvp PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues of the protein substrate. This information can be used to design protease inhibitors and possible antiviral drugs. | |||
Molecular modeling of the HIV-1 protease and its substrate binding site.,Weber IT, Miller M, Jaskolski M, Leis J, Skalka AM, Wlodawer A Science. 1989 Feb 17;243(4893):928-31. PMID:2537531<ref>PMID:2537531</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Weber, I T]] | [[Category: Weber, I T]] | ||