- Protein Classification
- Protein Links
 | extracellular side |
| cytoplasmic side |
| 1xq8 » Alpha-synuclein | |
|---|---|
| Depth | 8.7 ± 1.1 Å |
| Tilt Angle | 87 ± 4° |
| ΔGtransfer | -15.7 kcal/mol |
| Links to 1xq8 | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | cytoplasmic |
| Resolution | NMR |
| Other PDB entries of this protein | 2kkw |
| Number of subunits | 1 |
| Experimental Verification for 1xq8 » Alpha-synuclein |
|---|
| This is structure in micelles. The helices must rearrange to fit the plane. According to spin-labeling data, residues T59, V63, G67, V70, V74, V77, T81, A85 and A89 are buried in the hydrophobic interior of the membrane, while residues E61, N65, G68, T72, A76, Q79, and E83 are exposed to water in the membrane-bound state (Jao et al. 2004). |
| 1 reference |
|---|
| Jao, C.C., Der-Sarkissian, A., Chen, J., and Langen, R. 2004. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc. Natl. Acad. Sci. U. S. A. 101:8331-8336. PubMed |
| Comments on 1xq8 » Alpha-synuclein |
|---|
| The protein is involved in the regulation of dopamine release and transport. Normally, this is a soluble protein, localized primarily at the presynaptic region of axons. However it can also form filamentous aggregates that are that are involved in several neurodegenerative diseases. This structure is probably a misfolded state, which is formed in the presence of detergents or in lipid bilayers. |
