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Probing the Role of Backbone Hydrogen Bonding in a Critical β Sheet of the Extracellular Domain of a Cys‐Loop Receptor
Authors:Kristin R. Gleitsman  Henry A. Lester Dr.  Dennis A. Dougherty Dr.
Affiliation:1. Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91106 (USA), Fax: (+1)?626‐564‐9297;2. Division of Biology, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91106 (USA)
Abstract:Probing the sheet : The network of hydrogen bonds formed in the outer β sheet of the nicotinic acetylcholine receptor (nAChR; see figure) is fairly robust and tolerates single amide‐to‐ester mutations throughout. However, eliminating two proximal hydrogen bonds completely destroys receptor function; this adds further support to gating models that ascribe important roles to these β strands of the nAChR extracellular domain.
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Keywords:allosterism  backbone esters  ion channels  mutagenesis  receptors
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