- Protein Classification
- Protein Links
| 1rer » Fusion glycoprotein E1 | |
|---|---|
| Hydrophobic Thickness | 2.6 ± 2.0 Å |
| Tilt Angle | 38 ± 5° |
| ΔGtransfer | -6.5 kcal/mol |
| Links to 1rer | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | 3.2 Å |
| Other PDB entries of this protein | 1dyl, 1i9w, 1vcq, 2ala, 2v33 |
| Number of TM subunits | 3 |
| Experimental Verification for 1rer » Fusion glycoprotein E1 |
|---|
| Structures of mononers in the trimer are slightly different. The symmetry axis of the trimer is strongly tilted. It is also tilted according to EM data. A really symmetric structure is a pentamer of the trimers (Gibbons et al. 2004). |
| 1 reference |
|---|
| Gibbons DL, Vaney MC, Roussel A, Vigouroux A, Reilly B, Lepault J, Kielian M, Rey FA. 2004. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature. 427: 320-5. PubMed |
| Comments on 1rer » Fusion glycoprotein E1 |
|---|
| E1 is a class II viral fusion protein. This trimeric (low-pH-iduced) form is fusion active, and promotes release of viral nucleocapsid in cytoplasm after cell and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. N-terminal domain of this protein: 1dyl(NMR), 1vcp, 1vcq. |
