Structure of small hydrophobic protein from HMPV
3D Structure
| Method | Downloads |
|---|---|
| AlphaFold 3 | Click here |
Functional Information
Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
Interactions
- Interacts with glycoprotein G (via N-terminus). Interacts with protein M2-1; this interaction directs the matrix protein localization to cytoplasmic inclusions comprising viral proteins L, N, P, and M2-1 and mediates the matrix protein association with the nucleocapsid.
Post-Translational Modification
- Threonine 205 is phosphorylated to become phosphotheronine.
Domains orgainzation
- Region 1-110 = Interaction with M2-1By similarity
- Region 110-183 = Nuclear targeting and binding to host importin KPNB1By similarity
- Motif 194-206 = Nuclear export signal