Solution Structure of Apocalmodulin bound to a Binding Domain Peptide from the IQ motifs of Myosin V
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The solution structures of complexes between apocalmodulin （apoCaM） and a binding domain of the IQmotifs of myosin V have been determined by small-angle X-ray scattering （SAXS） with use of synchrotronradiation as an intense and stable X-ray source. We used three synthetic peptides of residues 772-786 （IQ1）,795-810 （IQ2）, and 772-810 （IQ（1+2）） of the myosin V to compare the solution structures with thecorresponding crystal structure （PDB: 2ix7）. The radius of gyration of apoCaM bound to the IQ1 or IQ2 ata molar ratio of 1:1 increased by 4.8±0.3Å or 3.8±0.3Å, respectively, as compared with the correspondingcrystal structure. The experimental Kratky plots indicated that apoCaM bound to the IQ1 or IQ2 adopts adumbbell-shaped structure. In contrast to these complexes, the solution of apoCaM/IQ（1+2） at a molar ratioof 2:1 became turbid, indicating that the solution contains several types of aggregates. The turbid solutionwas centrifuged and the supernatant was used for the SAXS measurements. The SAXS results suggested thatthe supernatant is composed of a mixture of apoCaM/IQ（1+2） and apoCaM. The radius of gyration ofapoCaM/IQ（1+2） at a molar ratio of 1:2 increased by 0.8±0.6Å, as compared with the corresponding crystalstructure. The experimental Kratky plot was compared with calculated curves of both solution structuresbased on the dumbbell-shaped structure and the crystal structure.
- 山形大学の論文
- 2010-02-15
山形大学 | 論文
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