Download MendeleyCatalytic 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, J.L., Hosur, M.V.(2009) PLoS One 4: E7860
- PubMed: 19924250
- DOI: https://doi.org/10.1371/journal.pone.0007860
- Primary Citation of Related Structures:
2WHH - PubMed Abstract:
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.
Organizational Affiliation:
Solid State Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai, India.
