Accurate Prediction of DnaK-Peptide Binding via Homology Modelling and Experimental Data Export

@article{citeulike:5540738, abstract = {Author Summary Molecular chaperones are essential elements of the protein quality control machinery that governs translocation and folding of nascent polypeptides, refolding and degradation of misfolded proteins, and activation of a wide range of client proteins. This variety of functions results from the existence of multiple chaperones with different structures. Chaperones bind to exposed regions of proteins to fulfil their function. The chaperone must hereby recognise a certain signal sequence on the substrate protein. The nature of the sequence that is exposed will determine the types of chaperones that can interact with it, and in the end will also determine the fate of the substrate protein: refolding, translocation, degradation or activation. Knowledge of the binding sequence determinants of molecular chaperones will shed more light on the mechanism of how each chaperone contributes to the cellular protein quality control system. In this study we have made an algorithm which accurately predicts binding sites for the well studied E. coli Hsp70 chaperone, DnaK, which is implicated in folding efficiency and prevention of aggregation. The ability to detect and design high-affinity DnaK binding sites enhances our understanding of chaperone-substrate recognition and opens great opportunities to enhance protein solubility using protein-DnaK binding motif fusions.}, author = {Van Durme, Joost and Maurer-Stroh, Sebastian and Gallardo, Rodrigo and Wilkinson, Hannah and Rousseau, Frederic and Schymkowitz, Joost}, citeulike-article-id = {5540738}, citeulike-linkout-0 = {http://dx.doi.org/10.1371/journal.pcbi.1000475}, day = {21}, doi = {10.1371/journal.pcbi.1000475}, journal = {PLoS Comput Biol}, keywords = {aggregation, chaperone, hsp70, predictive\_biology, protein\_folding}, month = {August}, number = {8}, pages = {e1000475+}, posted-at = {2009-08-21 21:08:47}, priority = {2}, publisher = {Public Library of Science}, title = {Accurate Prediction of DnaK-Peptide Binding via Homology Modelling and Experimental Data}, url = {http://dx.doi.org/10.1371/journal.pcbi.1000475}, volume = {5}, year = {2009} }

TY - JOUR ID - citeulike:5540738 L3 - citeulike-article-id:5540738 N2 - Author Summary Molecular chaperones are essential elements of the protein quality control machinery that governs translocation and folding of nascent polypeptides, refolding and degradation of misfolded proteins, and activation of a wide range of client proteins. This variety of functions results from the existence of multiple chaperones with different structures. Chaperones bind to exposed regions of proteins to fulfil their function. The chaperone must hereby recognise a certain signal sequence on the substrate protein. The nature of the sequence that is exposed will determine the types of chaperones that can interact with it, and in the end will also determine the fate of the substrate protein: refolding, translocation, degradation or activation. Knowledge of the binding sequence determinants of molecular chaperones will shed more light on the mechanism of how each chaperone contributes to the cellular protein quality control system. In this study we have made an algorithm which accurately predicts binding sites for the well studied E. coli Hsp70 chaperone, DnaK, which is implicated in folding efficiency and prevention of aggregation. The ability to detect and design high-affinity DnaK binding sites enhances our understanding of chaperone-substrate recognition and opens great opportunities to enhance protein solubility using protein-DnaK binding motif fusions. IS - 8 JF - PLoS Comput Biol TI - Accurate Prediction of DnaK-Peptide Binding via Homology Modelling and Experimental Data PB - Public Library of Science VL - 5 SP - e1000475 KW - aggregation KW - chaperone KW - hsp70 KW - predictive_biology KW - protein_folding AU - Van Durme, Joost AU - Maurer-Stroh, Sebastian AU - Gallardo, Rodrigo AU - Wilkinson, Hannah AU - Rousseau, Frederic AU - Schymkowitz, Joost PY - 2009/08/21/ UR - http://dx.doi.org/10.1371/journal.pcbi.1000475 ER -