Tools
ToolsSöder, Stephan and Pöschl, Ernst (2004) The NC1 domain of human collagen IV is necessary to initiate triple helix formation. Biochemical and Biophysical Research Communications, 325 (1). pp. 276-280. ISSN 1090-2104
Full text not available from this repository. (Request a copy)Abstract
Type IV collagen is a heterotrimeric molecule, which contains the N-terminal 7S, a central triple-helical domain, and the globular C-terminal NC1 domain. A zipper-like mechanism of triple helix formation, starting from the C-terminus, has been proposed for most collagens but for collagen type IV there has only been indirect evidence so far. In this study we expressed trimeric human collagen type IV to compare the effects of different structural variants on the formation of collagen IV molecules. Our data show that the NC1 but not 7S domain is essential for the chain association and initiation of triple helix formation. This strongly suggests an N-to-C terminal mechanism of triple helix formation. Additionally, we could show that the human α2(IV) chain can form chimeric α1.α1.α2(IV) heterotrimers with mouse subunits when expressed in PF-HR9 cells.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Cells and Tissues |
| Depositing User: | EPrints Services |
| Date Deposited: | 01 Oct 2010 13:37 |
| Last Modified: | 24 Sep 2024 10:07 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/1109 |
| DOI: | 10.1016/j.bbrc.2004.10.034 |
Actions (login required)
 |
View Item |