Structural insight into host plasma membrane association and assembly of HIV-1 matrix protein.

ABSTRACT: Oligomerization of Pr55^Gag is a critical step of the late stage of the HIV life cycle. It has been known that the binding of IP6, an abundant endogenous cyclitol molecule at the MA domain, has been linked to the oligomerization of Pr55^Gag. However, the exact binding site of IP6 on MA remains unknown and the structural details of this interaction are missing. Here, we present three high-resolution crystal structures of the MA domain in complex with IP6 molecules to reveal its binding mode. Additionally, extensive Differential Scanning Fluorimetry analysis combined with cryo- and ambient-temperature X-ray crystallography and GNM-based transfer entropy calculations identify the key residues that participate in IP6 binding. Our data provide novel insights about the multil

SUBMITTER: Ciftci H 

PROVIDER: S-EPMC8339130 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature