2q3k: Difference between revisions

Revision as of 19:35, 21 February 2008

Crystal Structure of Lysine Sulfonamide Inhibitor Reveals the Displacement of the Conserved Flap Water Molecule in HIV-1 Protease

OverviewOverview

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.

About this StructureAbout this Structure

2Q3K is a Single protein structure of sequence from Human immunodeficiency virus 1 with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of lysine sulfonamide inhibitor reveals the displacement of the conserved flap water molecule in human immunodeficiency virus type 1 protease., Nalam MN, Peeters A, Jonckers TH, Dierynck I, Schiffer CA, J Virol. 2007 Sep;81(17):9512-8. Epub 2007 Jun 27. PMID:17596316

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Human immunodeficiency virus 1]]
 [[Category: Single protein]]
-[[Category: Nalam, M.N.L.]]
+[[Category: Nalam, M N.L.]]
-[[Category: Schiffer, C.A.]]
+[[Category: Schiffer, C A.]]
 [[Category: ACT]]
 [[Category: MUW]]
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 [[Category: viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:06:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:35:32 2008''