Open AccessPreliminary X‐ray crystallographic studies of mouse UPR responsive protein P58(IPK) TPR fragment
Author(s) -
Tao Jiahui,
Wu Yunkun,
Ron David,
Sha Bingdong
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108000833
Subject(s) - unfolded protein response , protein folding , endoplasmic reticulum , crystallography , chaperone (clinical) , chemistry , biophysics , biology , biochemistry , medicine , pathology
Endoplasmic reticulum (ER) stress induces the unfolded protein response (UPR), which can promote protein folding and misfolded protein degradation and attenuate protein translation and protein translocation into the ER. P58(IPK) has been proposed to function as a molecular chaperone to maintain protein‐folding homeostasis in the ER under normal and stressed conditions. P58(IPK) contains nine TPR motifs and a C‐terminal J‐domain within its primary sequence. To investigate the mechanism by which P58(IPK) functions to promote protein folding within the ER, a P58(IPK) TPR fragment without the C‐terminal J‐domain was crystallized. The crystals diffract to 2.5 Å resolution using a synchrotron X‐ray source. The crystals belong to space group P 2 1 , with unit‐cell parameters a = 83.53, b = 92.75, c = 84.32 Å, α = 90.00, β = 119.36, γ = 90.00°. There are two P58(IPK) molecules in the asymmetric unit, which corresponds to a solvent content of approximately 60%. Structure determination by MAD methods is under way.