HIV-1 Reverse Transcriptase: A Metamorphic Protein with Three Stable States.

ABSTRACT: There has been a steadily increasing appreciation of the fact that the relationship between protein sequence and structure is often sufficiently ambiguous to allow a single sequence to adopt alternative, stable folds. Living organisms have been able to utilize such metamorphic proteins in remarkable and unanticipated ways. HIV-1 reverse transcriptase is among the earliest such proteins identified and remains a unique example in which a functional heterodimer contains two, alternatively folded polymerase domains. Structural characterization of the p66 precursor protein combined with NMR spectroscopic and molecular modeling studies have provided insights into the factors underlying the metamorphic transition and the subunit-specific programmed unfolding step required to expose the protease c

SUBMITTER: London RE 

PROVIDER: S-EPMC6686890 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature