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NMR structure of a full‐length single‐pass membrane protein NRADD
Author(s) -
Nadezhdin Kirill D.,
Goncharuk Sergey A.,
Arseniev Aleksander S.,
Mineev Konstantin S.
Publication year - 2019
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25703
Subject(s) - biophysics , transmembrane domain , transmembrane protein , crystallography , chemistry , domain (mathematical analysis) , model lipid bilayer , protein structure , nuclear magnetic resonance , membrane , receptor , physics , biology , biochemistry , lipid bilayer , mathematics , mathematical analysis , lipid bilayer phase behavior
Structural study of any single‐pass membrane protein is both an important and challenging task. In this report, we present the structure of a neurotrophin receptor‐alike death‐domain protein. The structure and dynamics of the protein was investigated by conventional nuclear magnetic resonance techniques in the solution of phospholipid bicelles. The receptor contains two folded regions—α‐helical transmembrane domain and globular C‐terminal death domain with more than 50% of the rest of backbone being disordered. This is the first structure of a full‐length single‐pass membrane receptor‐alike protein solved by the single method.