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.
I hypothesize that
Plasmodium falciparum has an Achilles' heel that can be attacked with
erythritol, the well-known sweetener that is classified as generally safe. Most
organisms have in their cell membrane two types of water-channel proteins:
aquaporins to maintain hydro-homeostasis across the memb...
We report on the results of a systematic survey of Halpha emission line stars
Covering 35 deg^2. It is distinguished by the combination of deep optical
Spectroscopy and long-term lightcurves that improve the certainty of our
Classifications. A total of 20 bona-fide symbiotic stars are found (13 S-ty...
We report the
First observation of the pressure-induced elimination of long-ranged AFM order
In LaMnPO single crystals that are iso-structural to the LaFeAsO
Superconductor15,17. By combining in-situ high pressure resistance and ac
Susceptibility measurements, we found that LaMnPO undergoes a crosso...
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