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Cover Feature: Probing the Interaction between HIV‐1 Protease and the Homodimeric p66/p66’ Reverse Transcriptase Precursor by Double Electron‐Electron Resonance EPR Spectroscopy (ChemBioChem 21/2020)
Author(s) -
Schmidt Thomas,
Louis John M.,
Clore G. Marius
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000697
Subject(s) - reverse transcriptase , rnase h , chemistry , protease , hiv 1 protease , cleavage (geology) , rna , virology , enzyme , biology , biochemistry , gene , paleontology , fracture (geology)
HIV‐1 reverse transcriptase catalyzes the conversion of single‐stranded viral RNA into proviral DNA prior to integration into the host genome. Reverse transcriptase is initially expressed as an asymmetric p66/p66′ homodimer precursor. Cleavage of a single RNase H domain in an open, accessible conformation by HIV‐1 protease yields the mature p66/p51 heterodimer. DEER‐derived probability distance distributions were used to directly probe the interaction of protease with the open state of the reverse transcriptase precursor. More information can be found in the communication by G. M. Clore et al.