X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.
In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 Å resolution. Interactions of the flexible N-term...
Saved in:
| Main Authors: | , , , , , , |
|---|---|
| Format: | article |
| Language: | EN |
| Published: |
Public Library of Science (PLoS)
2011
|
| Subjects: | |
| Online Access: | https://doaj.org/article/eaade0fab6c445af9f24313a60756608 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|