Structural highlights
FunctionGAG_HV1N5 Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu. Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity). Publication Abstract from PubMedSignificanceThe assembly of immature HIV-1 particles is initiated by targeting of the Gag polyproteins to the plasma membrane (PM). Gag binding to the PM is mediated by the N-terminally myristoylated matrix (myrMA) domain. Formation of a Gag lattice on the PM is obligatory for the assembly of immature HIV-1 and envelope (Env) incorporation. The structure of the myrMA lattice presented here provided insights on the molecular factors that stabilize the lattice and hence favor Env incorporation. Our data support a mechanism for Gag binding to the PM during the assembly of immature particles and upon maturation. These findings advance our understanding of a critical step in HIV-1 assembly. Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.,Samal AB, Green TJ, Saad JS Proc Natl Acad Sci U S A. 2022 Jun 7;119(23):e2200794119. doi:, 10.1073/pnas.2200794119. Epub 2022 Jun 3. PMID:35658080[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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