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2IF4

Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana

Summary for 2IF4
Entry DOI10.2210/pdb2if4/pdb
Related2F4E
DescriptorATFKBP42 (2 entities in total)
Functional Keywordsfkbp-like, alpha-beta, tpr-like, alpha, signaling protein
Biological sourceArabidopsis thaliana (thale cress)
Cellular locationCell membrane; Single-pass membrane protein: Q9LDC0
Total number of polymer chains1
Total formula weight38364.39
Authors
Granzin, J.,Eckhoff, A.,Weiergraeber, O.H. (deposition date: 2006-09-20, release date: 2006-10-31, Last modification date: 2024-02-21)
Primary citationGranzin, J.,Eckhoff, A.,Weiergraber, O.H.
Crystal Structure of a Multi-domain Immunophilin from Arabidopsis thaliana: A Paradigm for Regulation of Plant ABC Transporters.
J.Mol.Biol., 364:799-809, 2006
Cited by
PubMed 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.
PubMed: 17045295
DOI: 10.1016/j.jmb.2006.09.052
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.85 Å)
Structure validation

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