期刊
CHEMICO-BIOLOGICAL INTERACTIONS
卷 175, 期 1-3, 页码 303-304出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.cbi.2008.03.002
关键词
Conformational transitions; Fasciculin-2; Acetylcholinesterase
资金
- Howard Hughes Medical Institute Funding Source: Medline
Proteins have been metaphorically described - due to the introduction and extraordinary advances in biomolecular dynamics and computational biophysics over the past decades - as kicking and screaming molecules [G. Weber, Adv. Protein Chem. 29 (1975) 1-83]. In fact, dynamic fluctuations in protein structural conformation have been known to play an important role in protein function. However, fundamental mechanisms by which protein fluctuations couple with catalytic function of particular enzymes remain poorly understood. TO understand the dynamical properties of acetylcholinesterase (AChE) in rapid termination of cationic neurotransmitter, acetylcholine at neurosynaptic junctions, multiple molecular dynamics (MD) trajectories of AChE in the presence and absence of its inhibitors [J.M. Bui, J.A. McCammon, Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 15451-15456; J.M. Bui, Z. Radic, P. Taylor, J.A. McCammon, Biophys. J. 90 (2006) 3280-3287: J.M. Bui, K. Tai, J.A. McCammon, J. Am. Chem. Soc. 126 (2004) 7198-7205; J,M. Bui, R.H. Henchman, J.A. McCammon, Biophys. J. 85 (2003) 2267-2272] have been conducted and correlated with its inhibitory mechanisms. The intrinsic flexibilities of AChE, particularly of the long omega loop, are important in facilitating the ligand's inhibition of the enzyme. Published by Elsevier Ireland Ltd
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