2XS1

Crystal Structure of ALIX in complex with the SIVmac239 PYKEVTEDL Late Domain

Summary for 2XS1

• Entry DOI: 10.2210/pdb2xs1/pdb
• Related: 2XS8
• Descriptor: PROGRAMMED CELL DEATH 6-INTERACTING PROTEIN, GAG POLYPROTEIN (3 entities in total)
• Functional Keywords: protein transport-viral protein complex, cell cycle, protein transport/viral protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm, cytosol: Q8WUM4; Matrix protein p17: Virion (By similarity): Q76V78
• Total number of polymer chains: 2
• Total formula weight: 81259.28

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 citation

Zhai, 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

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

Experimental method

X-RAY DIFFRACTION (2.296 Å)