Abstract
The neurotrophins show a high degree of amino acid sequence homology, share similar solution properties, and display distinct but parallel functionalities. Here we report the crystallization and preliminary X-ray characterization of three neurotrophins: brain-derived neurotrophin, neurotrophin 3, and the heterodimer between brain-derived neurotrophin and neurotrophin 4. These findings are related to other published crystal parameters for neurotrophins, leading to the observation that, although crystal packing is highly variant, neurotrophins share common solubilities with respect to crystal growth.
| Original language | English |
|---|---|
| Pages (from-to) | 973-977 |
| Number of pages | 5 |
| Journal | Protein Science |
| Volume | 5 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 1996 |
| Externally published | Yes |
Keywords
- Trk
- crystallography
- nerve growth factor
- receptor
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology