Skeletal muscle myosin light chain kinase. A refined structural model.
A hydrodynamic, enzymatic and CD spectroscopic study of skeletal muscle myosin light chain kinase, three proteolytic fragments and corresponding complexes with calmodulin was performed. A refined shape model was built for the enzyme. It was shown that a head-and-tail structure is formed from two major fragments which are aligned end-to-end. The one fragment (Mr 36000) is compact, of high alpha-helix content and contains the catalytic center with the light chain and the calmodulin binding domains. The other fragment (Mr 33000) with unknown function is asymmetric (a/b greater than 10), of low alpha-helix and of unusually high proline content.
D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism; D002417:Cattle; D002942:Circular Dichroism; D008956:Models, Chemical; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009219:Myosin-Light-Chain Kinase; D011487:Protein Conformation; D011494:Protein Kinases / Q000032:analysis* / Q000378:metabolism; D011817:Rabbits
D002147:Calmodulin; D011494:Protein Kinases; D009219:Myosin-Light-Chain Kinase