Abstract
The complete primary structure of an integral membrane glycoprotein of the nuclear pore was deduced from the cDNA sequence. The cDNA encodes a polypeptide of 204,205 D containing a 25-residue-long signal sequence, two hydrophobic segments that could function as transmembrane segments, and 13 potential N-linked oligosaccharide addition sites. Endoglycosidase H reduces the molecular mass by approximately 9 kD suggesting that not all of these 13 sites are used. We discuss possible models for the topology of this protein in the pore membrane as well as a possible role in the formation of pores and pore complexes.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:18 p.m.) |
Deposited | 2 years, 1 month ago (July 21, 2023, 9:42 p.m.) |
Indexed | 2 weeks, 3 days ago (Aug. 5, 2025, 8:56 a.m.) |
Issued | 36 years, 2 months ago (June 1, 1989) |
Published | 36 years, 2 months ago (June 1, 1989) |
Published Online | 36 years, 2 months ago (June 1, 1989) |
Published Print | 36 years, 2 months ago (June 1, 1989) |
@article{Wozniak_1989, title={Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.}, volume={108}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.108.6.2083}, DOI={10.1083/jcb.108.6.2083}, number={6}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Wozniak, R W and Bartnik, E and Blobel, G}, year={1989}, month=jun, pages={2083–2092} }