Structural highlights
Publication Abstract from PubMed
Retroviral Gag proteins contain short late domain motifs that recruit cellular ESCRT pathway proteins to facilitate virus budding. ALIX-binding late domains often contain the core consensus sequence: "YPXnL" (where Xn can vary in sequence and length). However, some SIV Gag proteins lack this consensus sequence, yet still bind ALIX. We mapped divergent, ALIX-binding late domains within the p6(Gag) proteins of SIVmac239 (40SREKPYKEVTEDLLHLNSLF59) and SIVagmTan-1 (24AAGAYDPARKLLEQYAKK41). Crystal structures revealed that anchoring tyrosines (bold) and nearby hydrophobic residues (underlined) contact the ALIX V domain, revealing how lentiviruses employ a diverse family of late domain sequences to bind ALIX and promote virus budding.
Identification and Structural Characterization of the ALIX-Binding Late Domains of SIVmac239 and SIVagmTan-1.,Zhai Q, Landesman M, Robinson H, Sundquist WI, Hill CP J Virol. 2010 Oct 20. PMID:20962096[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhai Q, Landesman M, Robinson H, Sundquist WI, Hill CP. Identification and Structural Characterization of the ALIX-Binding Late Domains of SIVmac239 and SIVagmTan-1. J Virol. 2010 Oct 20. PMID:20962096 doi:10.1128/JVI.01683-10
