| id |
pubmed-2115101
|
| recordtype |
oai_dc
|
| spelling |
pubmed-21151012008-05-01 Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers Articles The influenza virus hemagglutinin (HA) is a well-characterized integral membrane glycoprotein composed of three identical subunits. We have analyzed the formation of mixed trimers in cells expressing two different HA gene products. The results show efficient and essentially random assembly of functional hybrid trimers provided that the HAs are from the same HA subtype. Trimerization is thus a posttranslational event, and subunits are recruited randomly from a common pool of monomers in the endoplasmic reticulum. Mixed trimers were not observed between HAs derived from different subtypes, indicating that the trimerization event is sequence specific. Mixed trimers containing mutant subunits were, moreover, used to establish that the acid-induced conformational change involved in the membrane fusion activity of HA is a highly cooperative event. The Rockefeller University Press 1988-03-01 /pmc/articles/PMC2115101/ /pubmed/3279048 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/).
|
| repository_type |
Open Access Journal
|
| institution_category |
Foreign Institution
|
| institution |
US National Center for Biotechnology Information
|
| building |
NCBI PubMed
|
| collection |
Online Access
|
| language |
English
|
| format |
Online
|
| title |
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| spellingShingle |
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| title_short |
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| title_full |
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| title_fullStr |
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| title_full_unstemmed |
Posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| title_sort |
posttranslational oligomerization and cooperative acid activation of mixed influenza hemagglutinin trimers
|
| description |
The influenza virus hemagglutinin (HA) is a well-characterized integral membrane glycoprotein composed of three identical subunits. We have analyzed the formation of mixed trimers in cells expressing two different HA gene products. The results show efficient and essentially random assembly of functional hybrid trimers provided that the HAs are from the same HA subtype. Trimerization is thus a posttranslational event, and subunits are recruited randomly from a common pool of monomers in the endoplasmic reticulum. Mixed trimers were not observed between HAs derived from different subtypes, indicating that the trimerization event is sequence specific. Mixed trimers containing mutant subunits were, moreover, used to establish that the acid-induced conformational change involved in the membrane fusion activity of HA is a highly cooperative event.
|
| publisher |
The Rockefeller University Press
|
| publishDate |
1988
|
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115101/
|
| _version_ |
1611413621272739840
|