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IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating.

ABSTRACT: The mechanisms that drive formation of the HIV capsid, first as an immature particle and then as a mature protein shell, remain incompletely understood. Recent discoveries of positively-charged rings in the immature and mature protein hexamer subunits that comprise them and their binding to the cellular metabolite inositol hexakisphosphate (IP6) have stimulated exciting new hypotheses. In this paper, we discuss how data from multiple structural and biochemical approaches are revealing potential roles for IP6 in the HIV-1 replication cycle from assembly to uncoating.

SUBMITTER: Dick RA

PROVIDER: S-EPMC6267275 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating.

Dick Robert A RA Mallery Donna L DL Vogt Volker M VM James Leo C LC

Viruses 20181115 11

The mechanisms that drive formation of the HIV capsid, first as an immature particle and then as a mature protein shell, remain incompletely understood. Recent discoveries of positively-charged rings in the immature and mature protein hexamer subunits that comprise them and their binding to the cellular metabolite inositol hexakisphosphate (IP6) have stimulated exciting new hypotheses. In this paper, we discuss how data from multiple structural and biochemical approaches are revealing potential ...[more]

PMID: 30445742

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