Hayes, Nandini V. L. published the artcileSelective calcium-dependent interaction of calmodulin with the head domain of synapsin 1, SDS of cas: 70539-42-3, the publication is Biochemical Journal (1991), 275(1), 93-7, database is CAplus and MEDLINE.
The calcium-dependent regulatory protein calmodulin is a critical element in the machinery regulating exocytosis at nerve terminals. T. Okabe and K. Sobue (1987) showed that calmodulin interacts with one of the proteins intimately connected with the neuronal exocytotic process, i.e. synapsin 1. Here, the site at which calmodulin interacts with synapsin 1 was studied. It is possible to generate chem. crosslinked Ca2+-dependent complexes between synapsin 1 and calmodulin in vitro, and covalent crosslinking was used in conjunction with calmodulin affinity chromatog. to identify fragments of synapsin 1 that interact with calmodulin. Ca2+-dependent calmodulin binding is restricted to the head domain (residues 1-453 in bovine synapsin 1). Within this domain the binding site is located in a unique 11-kDa Staphylococcus aureus V8 proteinase-generated fragment. This fragment does not contain the site for cAMP-dependent phosphorylation and therefore does not represent the N terminus of the protein.
Biochemical Journal published new progress about 70539-42-3. 70539-42-3 belongs to alcohols-buliding-blocks, auxiliary class pyrrolidine,Ester,Amide,Inhibitor,Inhibitor, name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, and the molecular formula is C18H20N2O12, SDS of cas: 70539-42-3.
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