Identification of drivers for the metamorphic transition of HIV-1 reverse transcriptase.

ABSTRACT: Recent structural characterizations of the p51 and p66 monomers have established an important starting point for understanding the maturation pathway of the human immunodeficiency virus (HIV)-1 reverse transcriptase p66/p51 heterodimer. This process requires a metamorphic transition of the polymerase domain leading to formation of a p66/p66' homodimer that exists as a structural heterodimer. To better understand the drivers for this metamorphic transition, we have performed NMR studies of ¹⁵N-labeled RT216 - a construct that includes the fingers and most of the palm domains. These studies are consistent with the conclusion that the p66 monomer exists as a spring-loaded complex. Initial dissociation of the fingers/palm : connection complex allows the fingers/palm to adopt an alte

SUBMITTER: Zheng X 

PROVIDER: S-EPMC5614878 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature