The Structure of the Neuropeptide Bradykinin Bound to the Human G‐Protein Coupled Receptor Bradykinin B2 as Determined by Solid‐State NMR Spectroscopy | Zendy

Lopez Jakob J. | Zendy; Shukla Arun K. | Zendy; Reinhart Christoph | Zendy; Schwalbe Harald | Zendy; Michel Hartmut | Zendy; Glaubitz Clemens | Zendy

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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.

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