Structure of the Human p115 Protein
Author Information
Author(s): Striegl Harald, Roske Yvette, Kümmel Daniel, Heinemann Udo
Primary Institution: Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany
Hypothesis
How does the structure of p115 facilitate its role in vesicular transport?
Conclusion
The study reveals the unique armadillo fold of p115, which is crucial for its function in vesicle tethering and protein interactions.
Supporting Evidence
- p115 is a stable homodimer that plays a key role in vesicle tethering.
- The structure of p115 includes a large globular head region and a long coiled-coil domain.
- The unique armadillo fold of p115 allows for multiple protein interactions.
Takeaway
Scientists studied a protein called p115 that helps transport things inside cells, and they found out how its shape helps it do its job.
Methodology
The researchers used X-ray crystallography to determine the structure of the globular head region of p115.
Limitations
The observed crystallographic dimer may not accurately reflect the protein structure in the cell.
Digital Object Identifier (DOI)
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