title: Spatial relationship between SH1 and the actin binding site on myosin subfragment-1 surface.
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 A.
mesh_terms: D000199:Actins / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001360:Avidin / Q000378:metabolism; D001665:Binding Sites; D001710:Biotin / Q000031:analogs & derivatives / Q000378:metabolism; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002498:Centrifugation; D011232:Chemical Precipitation; D009132:Muscles / Q000032:analysis; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000378:metabolism*
chemical_list: D000199:Actins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D001360:Avidin; D001710:Biotin; C043329:N-iodoacetyl-N'-biotinylhexylenediamine; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; C026049:EDTA-ATPase; D009218:Myosins; D000252:Calcium-Transporting ATPases