Structure of Human Calreticulin Globular Domain
Author Information
Author(s): Chouquet Anne, Païdassi Helena, Ling Wai Li, Frachet Philippe, Houen Gunnar, Arlaud Gérard J., Gaboriaud Christine
Primary Institution: Institut de Biologie Structurale Jean-Pierre Ebel, CEA, Grenoble, France
Hypothesis
What is the structure of the human calreticulin globular domain and how does it interact with peptides?
Conclusion
The study reveals a new peptide-binding site on the human calreticulin globular domain, suggesting a multi-molecular mechanism for its function.
Supporting Evidence
- The crystal structure was solved at 1.55 Å resolution.
- Interactions of the flexible N-terminal extension with the edge of the lectin site were observed.
- A calreticulin molecular zipper was identified in the crystal lattices.
Takeaway
Scientists looked at a part of a protein called calreticulin to see how it holds onto other tiny pieces. They found a new spot where it can grab onto these pieces, which helps it do its job better.
Methodology
The researchers solved the X-ray structure of the human calreticulin globular domain at a resolution of 1.55 Å.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website