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2XS8

Crystal Structure of ALIX in complex with the SIVagmTan-1 AYDPARKLL Late Domain

Summary for 2XS8
Entry DOI10.2210/pdb2xs8/pdb
DescriptorPROGRAMMED CELL DEATH 6-INTERACTING PROTEIN, SIVAGMTAN-1 GAG P6 (3 entities in total)
Functional Keywordsprotein transport-viral protein complex, cell cycle, protein transport/viral protein
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationCytoplasm, cytosol: Q8WUM4
Total number of polymer chains2
Total formula weight80833.85
Authors
Zhai, Q.,Landesman, M.,Robinson, H.,Sundquist, W.I.,Hill, C.P. (deposition date: 2010-09-24, release date: 2010-11-03, Last modification date: 2023-12-20)
Primary citationZhai, Q.,Landesman, M.,Robinson, H.,Sundquist, W.I.,Hill, C.P.
Identification and Structural Characterization of the Alix-Binding Late Domains of Sivmac239 and Sivagmtan-1.
J.Virol., 85:632-, 2011
Cited by
PubMed Abstract: 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.
PubMed: 20962096
DOI: 10.1128/JVI.01683-10
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.498 Å)
Structure validation

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