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dc.contributor.authorNalam, Madhavi N. L.
dc.contributor.authorPeeters, Anik
dc.contributor.authorJonckers, Tim H. M.
dc.contributor.authorDierynck, Inge
dc.contributor.authorSchiffer, Celia A.
dc.date2022-08-11T08:09:32.000
dc.date.accessioned2022-08-23T16:34:56Z
dc.date.available2022-08-23T16:34:56Z
dc.date.issued2007-06-29
dc.date.submitted2009-03-16
dc.identifier.citation<p>J Virol. 2007 Sep;81(17):9512-8. Epub 2007 Jun 27. <a href="http://dx.doi.org/10.1128/JVI.00799-07">Link to article on publisher's site</a></p>
dc.identifier.issn0022-538X (Print)
dc.identifier.doi10.1128/JVI.00799-07
dc.identifier.pmid17596316
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38446
dc.description.abstractHuman immunodeficiency virus type 1 (HIV-1) protease has been continuously evolving and developing resistance to all of the protease inhibitors. This requires the development of new inhibitors that bind to the protease in a novel fashion. Most of the inhibitors that are on the market are peptidomimetics, where a conserved water molecule mediates hydrogen bonding interactions between the inhibitors and the flaps of the protease. Recently a new class of inhibitors, lysine sulfonamides, was developed to combat the resistant variants of HIV protease. Here we report the crystal structure of a lysine sulfonamide. This inhibitor binds to the active site of HIV-1 protease in a novel manner, displacing the conserved water and making extensive hydrogen bonds with every region of the active site.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=17596316&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1951406/
dc.subjectBinding Sites
dc.subjectCrystallography, X-Ray
dc.subjectHIV Protease
dc.subjectHIV Protease Inhibitors
dc.subjectModels, Molecular
dc.subjectProtein Structure, Tertiary
dc.subjectSulfonamides
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleCrystal structure of lysine sulfonamide inhibitor reveals the displacement of the conserved flap water molecule in human immunodeficiency virus type 1 protease
dc.typeJournal Article
dc.source.journaltitleJournal of virology
dc.source.volume81
dc.source.issue17
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2313&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1314
dc.identifier.contextkey782987
refterms.dateFOA2022-08-23T16:34:56Z
html.description.abstract<p>Human immunodeficiency virus type 1 (HIV-1) protease has been continuously evolving and developing resistance to all of the protease inhibitors. This requires the development of new inhibitors that bind to the protease in a novel fashion. Most of the inhibitors that are on the market are peptidomimetics, where a conserved water molecule mediates hydrogen bonding interactions between the inhibitors and the flaps of the protease. Recently a new class of inhibitors, lysine sulfonamides, was developed to combat the resistant variants of HIV protease. Here we report the crystal structure of a lysine sulfonamide. This inhibitor binds to the active site of HIV-1 protease in a novel manner, displacing the conserved water and making extensive hydrogen bonds with every region of the active site.</p>
dc.identifier.submissionpathoapubs/1314
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages9512-8


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