Article
Magnetic resonance studies of the binding of oligonucleotide substrates to mutants of staphylococcal nuclease.
Proteins - 1 Jan 1994
Chuang W J, Gittis A G, Mildvan A S
Abstract excerpt
By a combination of NMR docking and model building, the substrate binding site on staphylococcal nuclease was found to accommodate a trinucleotide and to consist of three subsites, each interacting with a single nucleotidyl unit of DNA. Binding of the essential Ca2+ activator and substrate cleavage occur between subsites 1 and 2. Hence, catalytically productive binding would span subsites 1 and 2 while...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
