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Differential Effects of Hydrophobic Core Packing Residues for Thermodynamic and Mechanical Stability of a Hyperthermophilic Protein.
Langmuir
July 2016
School of Physics and Astronomy, ‡Astbury Centre for Structural and Molecular Biology, and §School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Proteins from organisms that have adapted to environmental extremes provide attractive systems to explore and determine the origins of protein stability. Improved hydrophobic core packing and decreased loop-length flexibility can increase the thermodynamic stability of proteins from hyperthermophilic organisms. However, their impact on protein mechanical stability is not known.
View Article and Find Full Text PDFDevelopmental immunolocalization of heat shock protein 70 (HSP70) in epithelial cell of rat kidney.
Histol Histopathol
November 2011
Kangwon National University Medical School, Chuncheon, Korea.
During renal development the cells in the medulla are exposed to elevated and variable interstitial osmolality. Heat shock protein 70 (HSP70) is a major molecular chaperone and plays an important role in the protection of cells in the renal medulla from high osmolality. The purpose of this study was to establish the time of immunolocalization and distribution of HSP70 in developing and adult rat kidney.
View Article and Find Full Text PDFLectin-like oxidized low-density lipoprotein receptor-1 delivers heat shock protein 60-fused antigen into the MHC class I presentation pathway.
J Immunol
August 2010
Gene Research Center, Institutes of Biomedical Science, Shanghai Medical College, Fudan University, Shanghai, China.
Heat shock protein (Hsp) 60 elicits a potent proinflammatory response in the innate immune system and has been proposed as a danger signal of stressed or damaged cells to the immune system. Previous studies reported CD14, TLR2, and TLR4 as mediators of signaling but probably not of binding. Although the receptor for Hsp60 was proposed to be saturable and specific on macrophages, it is not well defined.
View Article and Find Full Text PDFStructure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface.
Biochemistry
May 2003
Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900, USA.
J-domains are widespread protein interaction modules involved in recruiting and stimulating the activity of Hsp70 family chaperones. We have determined the crystal structure of the J-domain of auxilin, a protein which is involved in uncoating clathrin-coated vesicles. Comparison to the known structures of J-domains from four other proteins reveals that the auxilin J-domain is the most divergent of all J-domain structures described to date.
View Article and Find Full Text PDFCrystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima.
J Biol Chem
February 2003
Department of Molecular Cell Biology, Center for Molecular Medicine, SBRI, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
HtrA (high temperature requirement A), a periplasmic heat-shock protein, functions as a molecular chaperone at low temperatures, and its proteolytic activity is turned on at elevated temperatures. To investigate the mechanism of functional switch to protease, we determined the crystal structure of the NH(2)-terminal protease domain (PD) of HtrA from Thermotoga maritima, which was shown to retain both proteolytic and chaperone-like activities. Three subunits of HtrA PD compose a trimer, and multimerization architecture is similar to that found in the crystal structures of intact HtrA hexamer from Escherichia coli and human HtrA2 trimer.
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