Structural highlights
Function
PHOSP_SENDH Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N(0). Stabilizes the L protein upon binding it.
Publication Abstract from PubMed
The high resolution X-ray structure of the Sendai virus oligomerization domain reveals a homotetrameric coiled coil structure with many details that are different from classic coiled coils with canonical hydrophobic heptad repeats. Alternatives to the classic knobs-into-holes packing lead to differences in supercoil pitch and diameter that allow water molecules inside the core. This open and more hydrophilic structure does not seem to be destabilized by mutations that would be expected to disrupt classic coiled coils.
Tetrameric coiled coil domain of Sendai virus phosphoprotein.,Tarbouriech N, Curran J, Ruigrok RW, Burmeister WP Nat Struct Biol. 2000 Sep;7(9):777-81. PMID:10966649[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tarbouriech N, Curran J, Ruigrok RW, Burmeister WP. Tetrameric coiled coil domain of Sendai virus phosphoprotein. Nat Struct Biol. 2000 Sep;7(9):777-81. PMID:10966649 doi:10.1038/79013
