Home > Publications database > Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: A paradigm for regulation of plan ABC transporters |
Journal Article | PreJuSER-54327 |
; ;
2006
Elsevier
Amsterdam [u.a.]
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Please use a persistent id in citations: doi:10.1016/j.jmb.2006.09.052
Abstract: FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein.
Keyword(s): ATP-Binding Cassette Transporters: metabolism (MeSH) ; Arabidopsis Proteins: chemistry (MeSH) ; Crystallography, X-Ray (MeSH) ; Cytoplasm (MeSH) ; HSP90 Heat-Shock Proteins: metabolism (MeSH) ; Immunophilins: chemistry (MeSH) ; Molecular Structure (MeSH) ; Protein Binding (MeSH) ; Protein Conformation (MeSH) ; Tacrolimus Binding Proteins: chemistry (MeSH) ; ATP-Binding Cassette Transporters ; Arabidopsis Proteins ; HSP90 Heat-Shock Proteins ; TWD1 protein, Arabidopsis ; Tacrolimus Binding Proteins ; Immunophilins ; J ; FKBP42 (auto) ; Arabidopsis thaliana (auto) ; X-ray crystallography (auto) ; HSP90 (auto) ; ABC transporter (auto)
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