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Article

Effect of the active site D25N mutation on the structure, stability, and ligand binding of the mature HIV-1 protease.

The Journal of biological chemistry - 9 May 2008

Sayer Jane M, Liu Fengling, Ishima Rieko, Weber Irene T, Louis John M

Abstract excerpt

All aspartic proteases, including retroviral proteases, share the triplet DTG critical for the active site geometry and catalytic function. These residues interact closely in the active, dimeric structure of HIV-1 protease (PR). We have systematically assessed the effect of the D25N mutation on the structure and stability of the mature PR monomer and dimer. The D25N mutation (PR(D25N)) increases the equilibrium...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Enzyme Stability

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Share to Nuclear Magnetic Resonance, Biomolecular

Share to Structural Homology, Protein

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Identifiers

PMID: 18281688
DOI: 10.1074/jbc.M708506200
PMCID: PMC2442353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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