Home > Publications database > Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters |
Journal Article | PreJuSER-57966 |
; ;
2006
Elsevier
Amsterdam [u.a.]
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Please use a persistent id in citations: doi:10.1016/j.febslet.2005.12.007
Abstract: We present the three-dimensional structure of the N-terminal FK506-binding protein (FKBP)-like domain of the immunophilin FKBP42 from Arabidopsis thaliana. The data provide the structural background for the explanation of key functional properties reported previously.
Keyword(s): Arabidopsis: chemistry (MeSH) ; Arabidopsis: metabolism (MeSH) ; Arabidopsis Proteins: chemistry (MeSH) ; Arabidopsis Proteins: metabolism (MeSH) ; P-Glycoproteins: metabolism (MeSH) ; Protein Structure, Tertiary (MeSH) ; Structure-Activity Relationship (MeSH) ; Tacrolimus Binding Proteins: chemistry (MeSH) ; Tacrolimus Binding Proteins: metabolism (MeSH) ; Arabidopsis Proteins ; P-Glycoproteins ; TWD1 protein, Arabidopsis ; Tacrolimus Binding Proteins ; J ; Arabidopsis thaliana (auto) ; FKBP42 (auto) ; X-ray crystallography (auto)
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