Hi, I guess the following paper could be a good example. ''A leukotriene A4 hydrolase-related aminopeptidase from yeast undergoes induced fit upon inhibitor binding.''
http://www.ncbi.nlm.nih.gov/pubmed/21146536 Best regards, Mahmudul Hasan On Mon, Mar 3, 2014 at 6:33 PM, Gustavo Arruda <[email protected]>wrote: > Dear Jacob, > > we published in 2012 the structures of apo and peptide-bound forms of a > Dipeptidyl peptidase III: > > Proc Natl Acad Sci U S A. 2012 Apr 24;109(17):6525-30. doi: > 10.1073/pnas.1118005109. Epub 2012 Apr 9. > http://www.ncbi.nlm.nih.gov/pubmed/22493238 > > we observed a mainly rotational motion of approximately 60 degrees between > the two lobes of the enzyme upon peptide binding. > > Regards, > Gustavo > > Dr. Gustavo Arruda Bezerra > Group Djinovic > Department of Structural and Computational Biology > Max F. Perutz Laboratories > University of Vienna > Campus Vienna Biocenter 5 > A-1030 Vienna, > Austria > > http://www.mfpl.ac.at/ > > > Em Quinta-feira, 27 de Fevereiro de 2014 20:43, "Keller, Jacob" < > [email protected]> escreveu: > Dear Crystallographers, > > Does anyone know of good examples of large, reversible conformational > changes occurring between ligand-free and -bound states? Could also be a > non-relevant molecule binding, like sulfate or something inducing dubiously > -relevant changes. I already know of the calmodulin and periplasmic binding > protein families, but does anyone know of others out there? > > All the best, > > Jacob Keller > > ******************************************* > Jacob Pearson Keller, PhD > Looger Lab/HHMI Janelia Farms Research Campus > 19700 Helix Dr, Ashburn, VA 20147 > email: [email protected] > ******************************************* > >
