Tetrameric coiled coil domain of Sendai virus phosphoprotein

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 differe...

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Veröffentlicht in:Nature Structural Biology 2000-09, Vol.7 (9), p.777-781
Hauptverfasser: Tarbouriech, Nicolas, Curran, Joseph, Ruigrok, Rob W.H., Burmeister, Wilhelm P.
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Sprache:eng
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Zusammenfassung: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.
ISSN:1072-8368
1545-9993
1545-9985
DOI:10.1038/79013