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Catalytic water co-existing with a product peptide in the active site of HIV-1 protease revealed by X-ray structure analysis.

<div class='caption-title'>Difference density in the active site of HIV-1 protease/product complex.</div>
<div class='caption-title'>Fit of carboxy terminal product peptide and active site water molecules into 2Fo-Fc electron density.</div>
<div class='caption-title'>Hydrogen bonding interactions at the active site:</div>
Prashar V, Bihani S, Das A, Ferrer JL, Hosur M
OpenAccess logo PLoS One 4 e7860 (2009)
Cited: 2 times
EuropePMC logo PMID: 19924250

Abstract

Background

It is known that HIV-1 protease is an important target for design of antiviral compounds in the treatment of Acquired Immuno Deficiency Syndrome (AIDS). In this context, understanding the catalytic mechanism of the enzyme is of crucial importance as transition state structure directs inhibitor design. Most mechanistic proposals invoke nucleophilic attack on the scissile peptide bond by a water molecule. But such a water molecule coexisting with any ligand in the active site has not been found so far in the crystal structures.

Articles - 2whh mentioned but not cited (1)

  1. Catalytic water co-existing with a product peptide in the active site of HIV-1 protease revealed by X-ray structure analysis. Prashar V, Bihani S, Das A, Ferrer JL, Hosur M. PLoS One 4 e7860 (2009)


Reviews citing this publication (1)

  1. Linkers in the structural biology of protein-protein interactions. Reddy Chichili VP, Kumar V, Sivaraman J. Protein Sci 22 153-167 (2013)


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