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High affinity binding of hydrophobic and autoantigenic regions of proinsulin to the 70 kDa chaperone DnaK |
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| Authors: | Volker Burkart Rahel K Siegenthaler Elias Blasius Koen Vandenbroeck Iraide Alloza Waltraud Fingberg Nanette C Schloot Philipp Christen Hubert Kolb |
| Affiliation: | 1.German Diabetes Centre, Leibniz Institute at Heinrich Heine University Düsseldorf,Institute of Clinical Diabetology,Düsseldorf,Germany;2.Department of Biochemistry,University of Zurich,Zurich,Switzerland;3.Applied Genomics Research Group, McClay Research Center for Pharmaceutical Sciences,Queen's University,Belfast,UK;4.Research Group Immunobiology,Heinrich-Heine-University Düsseldorf,Düsseldorf,Germany |
| Abstract: | BackgroundChaperones facilitate proper folding of peptides and bind to misfolded proteins as occurring during periods of cell stress. Complexes of peptides with chaperones induce peptide-directed immunity. Here we analyzed the interaction of (pre)proinsulin with the best characterized chaperone of the hsp70 family, bacterial DnaK. |
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