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Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.
Barak D, Ordentlich A, Bromberg A, Kronman C, Marcus D, Lazar A, Ariel N, Velan B, Shafferman A. Barak D, et al. Among authors: ordentlich a. Biochemistry. 1995 Nov 28;34(47):15444-52. doi: 10.1021/bi00047a008. Biochemistry. 1995. PMID: 7492545
Replacement of residues Asp74, Trp286, and Tyr72, which are constituents of the peripheral anionic site (PAS) of human acetylcholinesterase (HuAChE), affected similarly both the binding and the inhibition constants of the PAS-specific ligand propidium, demonstrating that changes …
Replacement of residues Asp74, Trp286, and Tyr72, which are constituents of the peripheral anionic site (PAS) of human acetylcholinesterase …
Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core.
Barak D, Kronman C, Ordentlich A, Ariel N, Bromberg A, Marcus D, Lazar A, Velan B, Shafferman A. Barak D, et al. Among authors: ordentlich a. J Biol Chem. 1994 Mar 4;269(9):6296-305. J Biol Chem. 1994. PMID: 8119978 Free article.
The 6th PAS element residue Asp-74 is unique in its ability to affect conformation of both the active site and the PAS (Shafferman, A., Velan, B., Ordentlich, A., Kronman, C., Grosfeld, H., Leitner, M., Flashner, Y., Cohen, S., Barak, D., and Ariel, N. (1992) …
The 6th PAS element residue Asp-74 is unique in its ability to affect conformation of both the active site and the PAS (Shafferman, A …
49 results