6HTL
Measles Phosphoprotein Coiled-Coil Domain IPKI Variant
Summary for 6HTL
| Entry DOI | 10.2210/pdb6htl/pdb |
| Descriptor | Phosphoprotein, CALCIUM ION (3 entities in total) |
| Functional Keywords | coiled-coil, alpha helix, tetramer, 3-10 helix, viral protein |
| Biological source | Measles morbillivirus |
| Total number of polymer chains | 1 |
| Total formula weight | 8966.17 |
| Authors | Schramm, A.,Longhi, S. (deposition date: 2018-10-04, release date: 2019-06-05, Last modification date: 2024-01-24) |
| Primary citation | Bloyet, L.M.,Schramm, A.,Lazert, C.,Raynal, B.,Hologne, M.,Walker, O.,Longhi, S.,Gerlier, D. Regulation of measles virus gene expression by P protein coiled-coil properties. Sci Adv, 5:eaaw3702-eaaw3702, 2019 Cited by PubMed Abstract: The polymerase of negative-stranded RNA viruses consists of the large protein (L) and the phosphoprotein (P), the latter serving both as a chaperon and a cofactor for L. We mapped within measles virus (MeV) P the regions responsible for binding and stabilizing L and showed that the coiled-coil multimerization domain (MD) of P is required for gene expression. MeV MD is kinked as a result of the presence of a stammer. Both restoration of the heptad regularity and displacement of the stammer strongly decrease or abrogate activity in a minigenome assay. By contrast, P activity is rather tolerant of substitutions within the stammer. Single substitutions at the "a" or "d" hydrophobic anchor positions with residues of variable hydrophobicity revealed that P functionality requires a narrow range of cohesiveness of its MD. Results collectively indicate that, beyond merely ensuring P oligomerization, the MD finely tunes viral gene expression through its cohesiveness. PubMed: 31086822DOI: 10.1126/sciadv.aaw3702 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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