20962096
not annotated - annotated - LINNAEUS only
Identification and structural characterization of the ALIX-binding late domains of simian immunodeficiency virus SIVmac239 and SIVagmTan-1.
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 YPX(n)L (where X(n) can vary in sequence and length). However, some simian immunodeficiency virus (SIV) Gag proteins lack this consensus sequence, yet still bind ALIX. We mapped divergent, ALIX-binding late domains within the p6(Gag) proteins of SIV(mac239) ((40)SREKPYKEVTEDLLHLNSLF(59)) and SIV(agmTan-1) ((24)AAGAYDPARKLLEQYAKK(41)). Crystal structures revealed that anchoring tyrosines (in lightface) 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.
Ann file
T1 Species 83 122 simian immunodeficiency virus SIVmac239
N1 Reference T1 Taxonomy:11723
T2 Species 127 138 SIVagmTan-1
N2 Reference T2 Taxonomy:11723
T3 Out-of-scope 142 152 Retroviral
T4 Species 409 438 simian immunodeficiency virus
N4 Reference T4 Taxonomy:11723
T5 Species 440 443 SIV
N5 Reference T5 Taxonomy:11723
T6 Species 634 647 SIV(agmTan-1)
N6 Reference T6 Taxonomy:11723
T7 Species 587 598 SIV(mac239)
N3 Reference T3 Taxonomy:11632 Retroviridae