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| Title | The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. |
|---|---|
| Journal, issue, pages | J. Mol. Biol., Vol. 426, Page 150-168, Year 2014 |
| Publish date | Feb 11, 2013 (structure data deposition date) |
Authors | Skjevik, A.A. / Mileni, M. / Baumann, A. / Halskau, O. / Teigen, K. / Stevens, R.C. / Martinez, A. |
External links | J. Mol. Biol. / PubMed:24055376 |
| Methods | X-ray diffraction |
| Resolution | 3.08 Å |
| Structure data | ![]() PDB-4j6s: |
| Source |
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Keywords | HYDROLASE / 14-3-3 proteins / peptide binding / Dopamine synthesis / signal transduction / regulatory proteins / tyrosine hydroxylase / phosphorylation |
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