Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana
[FKB42_ARATH] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Modulates the uptake of MRP substrates into the vacuole; reduces metolachlor-GS (MOC-GS) and enhances 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG) uptake. Regulates cell elongation and orientation. Functions as a positive regulator of PGP1-mediated auxin transport. Confers drug modulation of PGP1 efflux activity as interaction with NPA or flavonol quercetin prevents its physical and functional interaction with PGP1. Required for the proper localization of auxin-related ABCB transporters. Plays a role in brassinosteroid (BR) signaling pathway.     
Publication Abstract from PubMed
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.
Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: a paradigm for regulation of plant ABC transporters.,Granzin J, Eckhoff A, Weiergraber OH J Mol Biol. 2006 Dec 8;364(4):799-809. Epub 2006 Sep 26. PMID:17045295
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.