Solution structure of the transmembrane domain of the mouse erythropoietin receptor in detergent micelles.

Abstract:

:Erythropoiesis is regulated by the erythropoietin receptor (EpoR) binding to its ligand. The transmembrane domain (TMD) and the juxtamembrane (JM) regions of the EpoR are important for signal transduction across the cell membrane. We report a solution NMR study of the mouse erythropoietin receptor (mEpoR) comprising the TMD and the JM regions reconstituted in dodecylphosphocholine (DPC) micelles. The TMD and the C-terminal JM region of the mEpoR are mainly α-helical, adopting a similar structure to those of the human EpoR. Residues from S216 to T219 in mEpoR form a short helix. Relaxation study demonstrates that the TMD of the mEpoR is rigid whilst the N-terminal region preceding the TMD is flexible. Fluorescence spectroscopy and sequence analysis indicate that the C-terminal JM region is exposed to the solvent. Helix wheel result shows that there is hydrophilic patch in the TMD of the mEpoR formed by residues S231, S238 and T242, and these residues might be important for the receptor dimerization.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Li Q,Wong YL,Yueqi Lee M,Li Y,Kang C

doi

10.1038/srep13586

subject

Has Abstract

pub_date

2015-08-28 00:00:00

pages

13586

issn

2045-2322

pii

srep13586

journal_volume

5

pub_type

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