background:
HIV1 performs highly complex orchestrated tasks during the assembly, budding, maturation and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. p55 is digested by HIV1 protease into intermediate products p41 and p15. p41 is further digested into matrix protein p17 and capsid protein p24. Likewise, p15 is further digested into nucleocapsid protein p7 and to p6 and p1.
Subunit:
Matrix protein p17, and probably Pr55Gag form hexamer rings of trimers. Oligomerization possibly creates a central hole into which the cytoplasmic tail of the gp41 envelope protein may be inserted. Pr55Gag interacts with host TRIM22; this interaction seems to disrupt proper trafficking of Gag polyprotein and may interfere with budding. p6-gag interacts with Vpr. p6-gag interacts with host TSG101. p6-gag interacts with host PDCD6IP/AIP1 (By similarity). Pr55Gag interacts with host PDZD8.
Subcellular Location:
Matrix protein p17: Virion (Potential). Host nucleus (By similarity). Host cytoplasm (By similarity). Host cell membrane; Lipid-anchor (Potential). Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane. Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential).
Similarity:
Belongs to the primate lentivirus group gag polyprotein family.
Contains 2 CCHSLCtype zinc fingers.
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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