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Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease by John M. Louis; Rieko Ishima; Annie Aniana; Jane M. Sayer is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Purification and __in vitro__ protein‐folding schemes were developed to produce monodisperse samples of the mature wild‐type HIV‐2 protease (PR2), enabling a comprehensive set of biochemical and biophysical studies to assess the dissociation of the dimeric protease. An E37K substitution in PR2 significantly retards autoproteolytic cleavage during expression. Furthermore, it permits convenient measurement of the dimer dissociation of PR2~E37K~ (elevated __K__~d~ ∼20 n__M__) by enzyme kinetics. Differential scanning calorimetry reveals a __T__~m~ of 60.5 for PR2 as compared with 65.7°C for HIV‐1 protease (PR1). Consistent with weaker binding of the clinical inhibitor darunavir (DRV) to PR2, the __T__~m~ of PR2 increases by 14.8°C in the presence of DRV as compared with 22.4°C for PR1. Dimer interface mutations, such as a T26A substitution in the active site (PR2~T26A~) or a deletion of the C‐terminal residues 96–99 (PR2~1–95~), drastically increase the __K__~d~ (>10^5^‐fold). PR2~T26A~ and PR2~1–95~ consist predominantly of folded monomers, as determined by nuclear magnetic resonance (NMR) and size‐exclusion chromatography coupled with multiangle light scattering and refr

Who reads Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease?

Author

John M. Louis; Rieko Ishima; Annie Aniana; Jane M. Sayer

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)