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Article

Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.

Proteins - 15 May 2009

Sayer Jane M, Louis John M

Abstract excerpt

The importance of the active site region aspartyl residues 25 and 29 of the mature HIV-1 protease (PR) for the binding of five clinical and three experimental protease inhibitors [symmetric cyclic urea inhibitor DMP323, nonhydrolyzable substrate analog (RPB) and the generic aspartic protease inhibitor acetyl-pepstatin (Ac-PEP)] was assessed by differential scanning calorimetry. DeltaT(m) values, defined as the...

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Identifiers

PMID: 18951411
DOI: 10.1002/prot.22271
PMCID: PMC2720045

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