PDBsum entry 2f4e

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Signaling protein PDB id
Protein chains
131 a.a.
Waters ×46

References listed in PDB file
Key reference
Title Crystal structure of a plant immunophilin domain involved in regulation of mdr-Type abc transporters.
Authors O.H.Weiergräber, A.Eckhoff, J.Granzin.
Ref. FEBS Lett, 2006, 580, 251-255. [DOI no: 10.1016/j.febslet.2005.12.007]
PubMed id 16364310
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.
Figure 1.
Fig. 1. Superposition of the crystal structures of AtFKBP42^1-180 (blue), HsFKBP12 (grey) and AtFKBP13 (orange). Secondary structure elements of the canonical FKBP fold are numbered consecutively; β0 is an additional β-strand present in AtFKBP42^1-180. The FK506 molecule bound to HsFKBP12 is shown as stick model.
Figure 3.
Fig. 3. Comparison of the molecular surfaces of HsFKBP12 (A) and AtFKBP42^1-180 (B). The FK506 ligand (dark grey) is positioned as in the complex with HsFKBP12. Orientation of the molecules is the same as in Fig. 2.
The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2006, 580, 251-255) copyright 2006.
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