FEBS Letters | |
Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F‐actin studied by 1H NMR spectroscopy | |
Kany, Harry1  Kalbitzer, Hans Robert1  Wolf, Jones1  | |
[1] University of Regensburg, Institute of Biophysics and Physical Biochemistry, Lehrstuhl Biologie III, Universitätsstr. 31, 93040 Regensburg, Germany | |
关键词: Nuclear magnetic resonance; Actin; Myosin; | |
DOI : 10.1016/S0014-5793(02)02855-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Mg-F-actin occurs in two conformational states, I and M, where the N-terminal amino acids are either immobile or highly mobile. In the rigor or ADP complex of rabbit myosin S1 with Mg-F-actin the N-terminal acetyl group of actin stays in its highly mobile state. The same is true for the complexes with the myosin motor domain from Dictyostelium discoideum. This excludes a direct strong interaction of the N-terminal amino acids with myosin in the rigor state as suggested. An interaction of the N-terminus of F-actin with myosin is also not promoted by occupying its low-affinity binding site(s) with divalent ions. The N-terminal high-mobility region may be part of a structural system which has evolved for releasing inadequate stress applied to the actin filaments
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020311906ZK.pdf | 127KB | download |