NMR structure of a full-length single-pass membrane protein NRADD.
 

NMR structure of a full-length single-pass membrane protein NRADD.

Related Articles NMR structure of a full-length single-pass membrane protein NRADD.

Proteins. 2019 Apr 29;:

Authors: Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS

Abstract
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, NRADD. 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 - ?-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. This article is protected by copyright. All rights reserved.


PMID: 31033000 [PubMed - as supplied by publisher]



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