title: Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase.
abstract: Small-angle X-ray and neutron scattering data were used to study the solution structure of calmodulin complexed with a synthetic peptide corresponding to residues 577-603 of rabbit skeletal muscle myosin light chain kinase. The X-ray data indicate that, in the presence of Ca2+, the calmodulin-peptide complex has a structure that is considerably more compact than uncomplexed calmodulin. The radius of gyration, Rg, for the complex is approximately 20% smaller than that of uncomplexed Ca2+.calmodulin (16 vs 21 A), and the maximum dimension, dmax, for the complex is also about 20% smaller (49 vs 67 A). The peptide-induced conformational rearrangement of calmodulin is [Ca2+] dependent. The length distribution function for the complex is more symmetric than that for uncomplexed Ca2+.calmodulin, indicating that more of the mass is distributed toward the center of mass for the complex, compared with the dumbell-shaped Ca2+.calmodulin. The solvent contrast dependence of Rg for neutron scattering indicates that the peptide is located more toward the center of the complex, while the calmodulin is located more peripherally, and that the centers of mass of the calmodulin and the peptide are not coincident. The scattering data support the hypothesis that the interconnecting helix region observed in the crystal structure for calmodulin is quite flexible in solution, allowing the two lobes of calmodulin to form close contacts on binding the peptide. This flexibility of the central helix may play a critical role in activating target enzymes such as myosin light chain kinase.
authors: Life Sciences Division and Neutron Scattering Center, Los Alamos National Laboratory, New Mexico 87545.
authors: D B
authors: DB
authors: Heidorn
authors: P A
authors: PA
authors: Seeger
authors: S E
authors: SE
authors: Rokop
authors: D K
authors: DK
authors: Blumenthal
authors: A R
authors: AR
authors: Means
authors: H
authors: H
authors: Crespi
authors: J
authors: J
authors: Trewhella
mesh_terms: D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism*; D002417:Cattle; D066298:In Vitro Techniques; D015394:Molecular Structure; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D011817:Rabbits; D012542:Scattering, Radiation
chemical_list: D002147:Calmodulin; D010446:Peptide Fragments; D009219:Myosin-Light-Chain Kinase