@article{oai:yamagata.repo.nii.ac.jp:00000919, author = {Izumi, Yoshinobu and Ebisawa, Hiroki and Jinbo, Yuji}, journal = {山形大学紀要. 工学 = Bulletin of Yamagata University. Engineering}, month = {Feb}, note = {論文(Article), The solution structures of complexes between apocalmodulin (apoCaM) and a binding domain of the IQ\nmotifs of myosin V have been determined by small-angle X-ray scattering (SAXS) with use of synchrotron\nradiation as an intense and stable X-ray source. We used three synthetic peptides of residues 772-786 (IQ1),\n795-810 (IQ2), and 772-810 (IQ(1+2)) of the myosin V to compare the solution structures with the\ncorresponding crystal structure (PDB: 2ix7). The radius of gyration of apoCaM bound to the IQ1 or IQ2 at\na molar ratio of 1:1 increased by 4.8±0.3A or 3.8±0.3A, respectively, as compared with the corresponding\ncrystal structure. The experimental Kratky plots indicated that apoCaM bound to the IQ1 or IQ2 adopts a\ndumbbell-shaped structure. In contrast to these complexes, the solution of apoCaM/IQ(1+2) at a molar ratio\nof 2:1 became turbid, indicating that the solution contains several types of aggregates. The turbid solution\nwas centrifuged and the supernatant was used for the SAXS measurements. The SAXS results suggested that\nthe supernatant is composed of a mixture of apoCaM/IQ(1+2) and apoCaM. The radius of gyration of\napoCaM/IQ(1+2) at a molar ratio of 1:2 increased by 0.8±0.6A, as compared with the corresponding crystal\nstructure. The experimental Kratky plot was compared with calculated curves of both solution structures\nbased on the dumbbell-shaped structure and the crystal structure.}, pages = {1--8}, title = {Solution Structure of Apocalmodulin bound to a Binding Domain Peptide from the IQ motifs of Myosin V}, volume = {32}, year = {2010} }