2R02: Crystal Structure Of Alix/aip1 In Complex With The Hiv-1 Ypltsl Late Domain

Retrovirus budding requires short peptide motifs (late domains) located within the viral Gag protein that function by recruiting cellular factors. The YPX(n)L late domains of HIV and other lentiviruses recruit the protein ALIX (also known as AIP1), which also functions in vesicle formation at the multivesicular body and in the abscission stage of cytokinesis. Here, we report the crystal structures of ALIX in complex with the YPX(n)L late domains from HIV-1 and EIAV. The two distinct late domains bind at the same site on the ALIX V domain but adopt different conformations that allow them to make equivalent contacts. Binding studies and functional assays verified the importance of key interface residues and revealed that binding affinities are tuned by context-dependent effects. These results reveal how YPX(n)L late domains recruit ALIX to facilitate virus budding and how ALIX can bind YPX(n)L sequences with both n = 1 and n = 3.
PDB ID: 2R02Download
MMDB ID: 61368
PDB Deposition Date: 2007/8/17
Updated in MMDB: 2007/12
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 2R02: dimeric; determined by author and by software (PISA)
Molecular Components in 2R02
Label Count Molecule
Proteins (2 molecules)
Programmed Cell Death 6-interacting Protein(Gene symbol: PDCD6IP)
Molecule annotation
Molecule annotation
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Citing MMDB