Title : Structural consequences of cyclophilin A binding on maturational refolding in human immunodeficiency virus type 1 capsid protein.

Pub. Date : 2001 May

PMID : 11312344






5 Functional Relationships(s)
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1 Here, we show that while CyP A binds both Gag and mature CA proteins, the two binding interactions are actually different. Glycosaminoglycans peptidylprolyl isomerase A Homo sapiens
2 Tryptophan 121 (W121) in CyP A distinguished the two proteins: a phenylalanine substitution (W121F) impaired binding of mature CA protein but not of Gag. Tryptophan peptidylprolyl isomerase A Homo sapiens
3 Tryptophan 121 (W121) in CyP A distinguished the two proteins: a phenylalanine substitution (W121F) impaired binding of mature CA protein but not of Gag. Phenylalanine peptidylprolyl isomerase A Homo sapiens
4 A structural consequence of Gag binding to CyP A was to block this maturational refolding, resulting in a 24-kDa CA protein retaining the immature Pro-rich loop conformation. Glycosaminoglycans peptidylprolyl isomerase A Homo sapiens
5 Binding to wild-type CyP A altered this conformation, as indicated by a reduction in the accessibility of Cys residue(s) in the region to chemical modification. Cysteine peptidylprolyl isomerase A Homo sapiens