Spatial relationship between SH1 and the actin binding site on myosin subfragment‐1 surface
- 15 October 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 176 (1), 75-78
- https://doi.org/10.1016/0014-5793(84)80914-x
Abstract
To examine the spatial relationship between SH1 thiol and actin binding site on subfragment-1 surface, we studied the interaction with actin of subfragment-1 whose SH1 was labeled with an iodoacetate derivative of biotin and covered with avidin. Subfragment-1-avidin complex bound F-actin and its Mg2+ ATPase activity was activated by actin. Considering the size and the location of biotin binding site on avidin, our results suggest that SH1 is separated from the actin binding site on subfragment-1 surface by at least 17–20 Å.Keywords
This publication has 6 references indexed in Scilit:
- Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex.Proceedings of the National Academy of Sciences, 1983
- Effect of bridging the two essential thiols of myosin on its spectral and actin-binding propertiesBiochemistry, 1976
- Interaction of actin with N-ethylmaleimide modified heavy meromyosin in the presence and absence of adenosine triphosphateBiochemistry, 1975
- Electron spin resonance of myosin spin labeled at the St thiol groups during hydrolysis of adenosine triphosphateArchives of Biochemistry and Biophysics, 1973
- The use of bifunctional biotinyl compounds to determine the arrangement of subunits in avidinBiochemical Journal, 1971
- The Active Site of Myosin Adenosine TriphosphatasePublished by Elsevier ,1962