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Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
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 potenti...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1989
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115607/ https://www.ncbi.nlm.nih.gov/pubmed/2738089 |
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collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2115607 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1989 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21156072008-05-01 Primary structure analysis of an integral membrane glycoprotein of the nuclear pore J Cell Biol Articles 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. The Rockefeller University Press 1989-06-01 /pmc/articles/PMC2115607/ /pubmed/2738089 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
title | Primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
title_full | Primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
title_fullStr | Primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
title_full_unstemmed | Primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
title_short | Primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
title_sort | primary structure analysis of an integral membrane glycoprotein of the nuclear pore |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115607/ https://www.ncbi.nlm.nih.gov/pubmed/2738089 |