NMR structure of a full-length single-pass membrane protein NRADD.
NRADD
bicelles
p75 neurotrophin receptor
solution NMR
structure
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
09 2019
09 2019
Historique:
received:
17
09
2018
revised:
05
04
2019
accepted:
23
04
2019
pubmed:
30
4
2019
medline:
19
5
2020
entrez:
30
4
2019
Statut:
ppublish
Résumé
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.
Substances chimiques
Membrane Proteins
0
Phospholipids
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
786-790Informations de copyright
© 2019 Wiley Periodicals, Inc.