A model for the solution structure of the rod arrestin tetramer. Export

@article{citeulike:5891797, abstract = {Visual rod arrestin has the ability to self-associate at physiological concentrations. We previously demonstrated that only monomeric arrestin can bind the receptor and that the arrestin tetramer in solution differs from that in the crystal. We employed the Rosetta docking software to generate molecular models of the physiologically relevant solution tetramer based on the monomeric arrestin crystal structure. The resulting models were filtered using the Rosetta energy function, experimental intersubunit distances measured with DEER spectroscopy, and intersubunit contact sites identified by mutagenesis and site-directed spin labeling. This resulted in a unique model for subsequent evaluation. The validity of the model is strongly supported by model-directed crosslinking and targeted mutagenesis that yields arrestin variants deficient in self-association. The structure of the solution tetramer explains its inability to bind rhodopsin and paves the way for experimental studies of the physiological role of rod arrestin self-association.}, author = {Hanson, Susan M. and Dawson, Eric S. and Francis, Derek J. and Van Eps, Ned and Klug, Candice S. and Hubbell, Wayne L. and Meiler, Jens and Gurevich, Vsevolod V.}, citeulike-article-id = {5891797}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.str.2008.03.006}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18547524}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18547524}, doi = {10.1016/j.str.2008.03.006}, issn = {0969-2126}, journal = {Structure (London, England : 1993)}, keywords = {arrestin, docking, modeling}, month = {June}, number = {6}, pages = {924--934}, posted-at = {2009-10-05 18:41:01}, priority = {2}, title = {A model for the solution structure of the rod arrestin tetramer.}, url = {http://dx.doi.org/10.1016/j.str.2008.03.006}, volume = {16}, year = {2008} }

TY - JOUR ID - citeulike:5891797 L3 - citeulike-article-id:5891797 N2 - Visual rod arrestin has the ability to self-associate at physiological concentrations. We previously demonstrated that only monomeric arrestin can bind the receptor and that the arrestin tetramer in solution differs from that in the crystal. We employed the Rosetta docking software to generate molecular models of the physiologically relevant solution tetramer based on the monomeric arrestin crystal structure. The resulting models were filtered using the Rosetta energy function, experimental intersubunit distances measured with DEER spectroscopy, and intersubunit contact sites identified by mutagenesis and site-directed spin labeling. This resulted in a unique model for subsequent evaluation. The validity of the model is strongly supported by model-directed crosslinking and targeted mutagenesis that yields arrestin variants deficient in self-association. The structure of the solution tetramer explains its inability to bind rhodopsin and paves the way for experimental studies of the physiological role of rod arrestin self-association. IS - 6 JF - Structure (London, England : 1993) SN - 0969-2126 EP - 934 TI - A model for the solution structure of the rod arrestin tetramer. VL - 16 SP - 924 KW - arrestin KW - docking KW - modeling AU - Hanson, Susan AU - Dawson, Eric AU - Francis, Derek AU - Van Eps, Ned AU - Klug, Candice AU - Hubbell, Wayne AU - Meiler, Jens AU - Gurevich, Vsevolod PY - 2008/06// UR - http://dx.doi.org/10.1016/j.str.2008.03.006 ER -