CRYSTAL STRUCTURE OF ALIX IN COMPLEX WITH THE SIVMAC239 PYKEVTEDL LATE DOMAINCRYSTAL STRUCTURE OF ALIX IN COMPLEX WITH THE SIVMAC239 PYKEVTEDL LATE DOMAIN

Structural highlights

2xs1 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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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

  1. 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

2xs1, resolution 2.30Å

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