2Q3K: Crystal Structure Of Lysine Sulfonamide Inhibitor Reveals The Displacement Of The Conserved Flap Water Molecule In Hiv-1 Protease

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.
PDB ID: 2Q3KDownload
MMDB ID: 60188
PDB Deposition Date: 2007/5/30
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 2Q3K: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2Q3K
Label Count Molecule
Proteins (2 molecules)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

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