Premium
The Structure of the Neuropeptide Bradykinin Bound to the Human G‐Protein Coupled Receptor Bradykinin B2 as Determined by Solid‐State NMR Spectroscopy
Author(s) -
Lopez Jakob J.,
Shukla Arun K.,
Reinhart Christoph,
Schwalbe Harald,
Michel Hartmut,
Glaubitz Clemens
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200704282
Subject(s) - bradykinin , neuropeptide , chemistry , spectroscopy , nuclear magnetic resonance spectroscopy , receptor , solid state nuclear magnetic resonance , g protein coupled receptor , amino acid , biophysics , crystallography , biochemistry , stereochemistry , nuclear magnetic resonance , biology , physics , quantum mechanics
Triggering the signal : The backbone structure of the nine amino acid neuropeptide bradykinin (see picture) bound to the human G‐protein coupled bradykinin subtype 2 receptor has been determined by solid‐state NMR spectroscopy. Torsion‐angle constraints based on 13 C chemical shifts were used for structure calculation, which revealed an elongated conformation with an α‐helical turn at the N terminus and a β turn at the C terminus.