The Library
Secondary structure, orientation, and oligomerization of phospholemman, a cardiac transmembrane protein
Tools
Beevers, Andrew J. and Kukol, Andreas (2006) Secondary structure, orientation, and oligomerization of phospholemman, a cardiac transmembrane protein. Protein Science, Vol.15 (No.5). pp. 1127-1132. doi:10.1110/ps.051899406 ISSN 0961-8368.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1110/ps.051899406
Abstract
Human phospholemman (PLM) is a 72-residue protein, which is expressed at high density in the cardiac plasma membrane and in various other tissues. It forms ion channels selective for K+, Cl-, and taurine in lipid bilayers and colocalizes with the Na+/K+-ATPase and the Na+/Ca2+-exchanger, which may suggest a role in the regulation of cell volume. Here we present the first structural data based on synthetic peptides representing the transmembrane domain of PLM. Perfluoro-octaneoate-PAGE of reconstituted proteoliposomes containing PLM reveals a tetrameric homo-oligomerization. Infrared spectroscopy of proteoliposomes shows that the PLM peptide is completely alpha-helical, even beyond the hydrophobic core residues. Hydrogen/deuterium exchange experiments reveal that a core of 20-22 residues is not accessible to water, thus embedded in the lipid membrane. The maximum helix tilt is 17 degrees +/- 2 degrees obtained by attenuated total reflection infrared spectroscopy. Thus, our data support the idea of ion channel formation by the PLM transmembrane domain.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
Journal or Publication Title: | Protein Science | ||||
Publisher: | John Wiley & Sons Ltd. | ||||
ISSN: | 0961-8368 | ||||
Official Date: | May 2006 | ||||
Dates: |
|
||||
Volume: | Vol.15 | ||||
Number: | No.5 | ||||
Number of Pages: | 6 | ||||
Page Range: | pp. 1127-1132 | ||||
DOI: | 10.1110/ps.051899406 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Open Access (Creative Commons) | ||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||
Grant number: | 88/B19450 |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |