Kany, Harry and Wolf, Jones and Kalbitzer, Hans Robert (2002) Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F-actin studied by H-1 NMR spectroscopy. FEBS LETTERS, 521 (1-3): PII S0014-. pp. 121-126. ISSN 0014-5793
Full text not available from this repository. (Request a copy)Abstract
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 Diciyostelium 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 (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEAR-MAGNETIC-RESONANCE; N-TERMINAL SEGMENT; LOW-AFFINITY SITES; X-RAY STRUCTURES; MOTOR DOMAIN; HEAVY-CHAIN; ACTOMYOSIN INTERACTIONS; INTERNAL MOTIONS; BINDING-SITES; PROTON NMR; nuclear magnetic resonance; actin; myosin |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 19 Oct 2021 07:06 |
| Last Modified: | 19 Oct 2021 07:06 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40152 |
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