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Photoaffinity Cross-Linking of the Corticotropin-Releasing Factor Receptor Type 1 with Photoreactive Urocortin Analogues

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Department of Peptide Chemistry, Institute of Molecular Pharmacology (FMP), 13125 Berlin, Germany, and Department of Pharmacology, Faculty of Medicine, Université de Sherbrooke (IPS), Sherbrooke, Quebec, Canada J1H 5N4
Cite this: Biochemistry 2005, 44, 47, 15569–15577
Publication Date (Web):November 3, 2005
https://doi.org/10.1021/bi0507027
Copyright © 2005 American Chemical Society

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    Abstract

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    Interaction of natural peptide ligands with class 2 GPCRs, which are targets of biologically important hormones such as glucagon, secretin, and corticotropin-releasing factor (CRF), occurs with a common orientation, in that the ligand C-terminus binds to the extracellular receptor N-terminus, whereas the ligand N-terminus binds to the receptor juxtamembrane domain. N-Terminal truncation, by eight amino acids in the case of CRF, leads to antagonists, suggesting those residues constitute the receptor activating sequence. Here, we identified by photoaffinity cross-linking using p-benzoyl-l-phenylalanine (Bpa) analogues of urocortin (Ucn) the most affine CRF receptor agonist, interaction domains of CRF1 receptor with Bpa residues at exclusive positions. Specific cleavage patterns of the corresponding ligand−receptor complexes, obtained using several cleavage methods in combination with SDS−PAGE for fragment size determination, showed that a Bpa group located N-terminally or in position 12 binds at the second and such in position 17 or 22 at the first extracellular receptor loop. Our results indicate that the very N-terminal ligand residues (1−11), which are responsible for receptor activation, are oriented to the juxtamembrane domain by interaction of amino acid residues 12, 17, and 22. Our findings contradict a recently proposed interaction model derived from ligand interaction with a soluble receptor N-terminus, indicating that conclusions drawn from such a reduced system may be of limited value to understand the interaction with the full-length receptor.

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     Address correspondence to this author. Phone:  +49(0)30-94793-240. Fax:  +49(0)30-94793-159. E-mail:  [email protected].

     Institute of Molecular Pharmacology.

    §

     Université de Sherbrooke.

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