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Active State-like Conformational Elements in the β₂-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs^†

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Daniel S. Han, Simon X. Wang and Harel Weinstein*

Department of Physiology and Biophysics, Weill Medical College, Cornell University, 1300 York Avenue, New York, New York 10021

Biochemistry, 2008, 47 (28), pp 7317–7321

DOI: 10.1021/bi800442g

Publication Date (Web): June 18, 2008

Copyright © 2008 American Chemical Society

†

This work was supported in part by NIH Grants P01 DA-012923 and T32 DA007274-14.

,

* To whom correspondence should be addressed. Phone: (212) 746-6358. Fax: (212) 746-8690. E-mail: haw2002@med.cornell.edu.

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Abstract

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G-Protein-coupled receptors (GPCRs) adopt various functionally relevant conformational states in cell signaling processes. Recently determined crystal structures of rhodopsin and the β₂-adrenergic receptor (β₂-AR) offer insight into previously uncharacterized active conformations, but the molecular states of these GPCRs are likely to contain both inactive and active-like conformational elements. We have identified conformational rearrangements in the dynamics of the TM7−HX8 segment that relate to the properties of the conserved NPxxY(x)5,6F motif and show that they can be used to identify active state-like conformational elements in the corresponding regions of the new structures of rhodopsin and the β₂-AR.

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History

Published In Issue July 15, 2008
Article ASAPJune 18, 2008
Received: March 14, 2008
Revised: April 30, 2008

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