Catalytic water co-existing with a product peptide in the active site of HIV-1 protease revealed by X-ray structure analysis.
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 inh...
Main Authors: | Vishal Prashar, Subhash Bihani, Amit Das, Jean-Luc Ferrer, Madhusoodan Hosur |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2009-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC2775671?pdf=render |
Similar Items
-
X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases.
by: Subhash C Bihani, et al.
Published: (2011-01-01) -
Identification of 3'-UTR single nucleotide variants and prediction of select protein imbalance in mesial temporal lobe epilepsy patients.
by: Tanusree Chaudhuri, et al.
Published: (2021-01-01) -
Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions
by: Chen Chaoping, et al.
Published: (2011-10-01) -
NMR insights into folding and self-association of Plasmodium falciparum P2.
by: Pushpa Mishra, et al.
Published: (2012-01-01) -
Synthetic Peptides as Structural Maquettes of Angiotensin-I Converting Enzyme Catalytic Sites
by: Zinovia Spyranti, et al.
Published: (2010-01-01)