HIV-1 Reverse Transcriptase: A Metamorphic Protein with Three Stable States
| Autor: | Robert E. London |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Protein Folding Molecular model Protein Conformation medicine.medical_treatment Cleavage (embryo) Article 03 medical and health sciences Protein sequencing Multienzyme Complexes Structural Biology Enzyme Stability medicine Ribonuclease Nuclear Magnetic Resonance Biomolecular Molecular Biology Polymerase 030304 developmental biology Stable state 0303 health sciences Protease biology Chemistry 030302 biochemistry & molecular biology HIV Reverse Transcriptase Reverse transcriptase Biochemistry HIV-1 biology.protein |
| Zdroj: | Structure. 27:420-426 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2018.11.011 |
| Popis: | 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 cleavage site within the ribonuclease H domain, supporting the conversion of the p66/p66' precursor into the mature p66/p51 heterodimer. |
| Databáze: | OpenAIRE |
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