Title : A zinc-binding region in Vif binds Cul5 and determines cullin selection.

Pub. Date : 2006 Jun 23

PMID : 16636053






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The HCCH zinc coordination site, which is conserved among primate lentivirus Vif proteins, does not correspond to any known class of zinc-binding motif. alpha-hexachlorocyclohexane Vif Human immunodeficiency virus 1
2 Mutations of His/Cys residues in the HCCH motif impair zinc coordination, Cul5 binding, and APOBEC3G degradation. alpha-hexachlorocyclohexane cullin 5 Homo sapiens
3 Mutations of His/Cys residues in the HCCH motif impair zinc coordination, Cul5 binding, and APOBEC3G degradation. alpha-hexachlorocyclohexane apolipoprotein B mRNA editing enzyme catalytic subunit 3G Homo sapiens
4 We propose that the HCCH zinc-binding motif facilitates Vif-Cul5 binding by playing a structural role in positioning hydrophobic residues for direct contact with Cul5. alpha-hexachlorocyclohexane Vif Human immunodeficiency virus 1
5 We propose that the HCCH zinc-binding motif facilitates Vif-Cul5 binding by playing a structural role in positioning hydrophobic residues for direct contact with Cul5. alpha-hexachlorocyclohexane cullin 5 Homo sapiens
6 We propose that the HCCH zinc-binding motif facilitates Vif-Cul5 binding by playing a structural role in positioning hydrophobic residues for direct contact with Cul5. alpha-hexachlorocyclohexane cullin 5 Homo sapiens