Use of an in situ disulfide cross-linking strategy to map proximities between amino acid residues in transmembrane domains I and VII of the M(sub)3 muscarinic acetylcholine receptor

The in situ disulfide cross-linking and the iodine cross-linking studies reveal that agonist activation of the M(sub)3 muscarinic receptor does not result in significant changes in the relative orientation of the outer and/or central segments of transmembrane domains I and VII. Further more, the relative orientations of TMI and VII differ among class 1 G protein-coupled receptors.