Identification of the protein kinase A regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking. Export

@article{anand2003, abstract = {An important goal after structural genomics is to build up the structures of higher-order protein-protein complexes from structures of the individual subunits. Often structures of higher order complexes are difficult to obtain by crystallography. We have used an alternative approach in which the structures of the individual catalytic (C) subunit and RIalpha regulatory (R) subunit of PKA were first subjected to computational docking, and the top 100,000 solutions were subsequently filtered based on amide hydrogen/deuterium (H/2H) exchange interface protection data. The resulting set of filtered solutions forms an ensemble of structures in which, besides the inhibitor peptide binding site, a flat interface between the C-terminal lobe of the C-subunit and the A- and B-helices of RIalpha is uniquely identified. This holoenzyme structure satisfies all previous experimental data on the complex and allows prediction of new contacts between the two subunits.}, address = {Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0378, USA.}, author = {Anand, G. S. and Law, D. and Mandell, J. G. and Snead, A. N. and Tsigelny, I. and Taylor, S. S. and Ten Eyck, L. F. and Komives, E. A.}, citeulike-article-id = {2646537}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.2232255100}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/14583592}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=14583592}, day = {11}, doi = {10.1073/pnas.2232255100}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {chapter, docking, nmr, ppi}, month = {November}, number = {23}, pages = {13264--13269}, posted-at = {2008-04-09 17:55:03}, priority = {2}, title = {Identification of the protein kinase A regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking.}, url = {http://dx.doi.org/10.1073/pnas.2232255100}, volume = {100}, year = {2003} }

TY - JOUR ID - anand2003 L3 - citeulike-article-id:2646537 N2 - An important goal after structural genomics is to build up the structures of higher-order protein-protein complexes from structures of the individual subunits. Often structures of higher order complexes are difficult to obtain by crystallography. We have used an alternative approach in which the structures of the individual catalytic (C) subunit and RIalpha regulatory (R) subunit of PKA were first subjected to computational docking, and the top 100,000 solutions were subsequently filtered based on amide hydrogen/deuterium (H/2H) exchange interface protection data. The resulting set of filtered solutions forms an ensemble of structures in which, besides the inhibitor peptide binding site, a flat interface between the C-terminal lobe of the C-subunit and the A- and B-helices of RIalpha is uniquely identified. This holoenzyme structure satisfies all previous experimental data on the complex and allows prediction of new contacts between the two subunits. IS - 23 JF - Proceedings of the National Academy of Sciences of the United States of America SN - 0027-8424 AD - Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0378, USA. EP - 13269 TI - Identification of the protein kinase A regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking. VL - 100 SP - 13264 KW - chapter KW - docking KW - nmr KW - ppi AU - Anand, GS AU - Law, D AU - Mandell, JG AU - Snead, AN AU - Tsigelny, I AU - Taylor, SS AU - Ten Eyck, LF AU - Komives, EA PY - 2003/11/11/ UR - http://dx.doi.org/10.1073/pnas.2232255100 ER -