Modulation of the affinity of aspartic proteases by the mutated residues in active site models

Amiram Goldblum*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The active sites of 3 types of aspartic proteases are modeled, based on crystallographic coordinates of endothiapepsin and of a model of HIV-1 protease. The enthalpies of deprotonation from neutral to mono-anion and to dianion are calculated with semiempirical minimal neglect of differential overlap, hydrogen bonding corrected (MNDO/H). This quantum mechanical study of models for the active sites of pepsins, human renin and retroviral aspartic proteases demonstrates that the replacements ofThr-218 from pepsins by Ala in human renin and of both Ser-35 and Thr-218 by alanines in retroviral proteases increases the proton affinity and modulates the charge distribution of those active sites compared to the pepsins.

Original languageAmerican English
Pages (from-to)241-244
Number of pages4
JournalFEBS Letters
Volume261
Issue number2
DOIs
StatePublished - 26 Feb 1990

Keywords

  • HIV-1
  • Model, molecular
  • Pepsin
  • Protease, Aspartic
  • Renin

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