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

Proteins. 2019 Sep;87(9):786-790. doi: 10.1002/prot.25703. Epub 2019 May 11.

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. 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.

Keywords: NRADD; bicelles; p75 neurotrophin receptor; solution NMR; structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Magnetic Resonance Spectroscopy
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Phospholipids / chemistry*
  • Phospholipids / metabolism

Substances

  • Membrane Proteins
  • Phospholipids