The crystal structure of a partial mouse Notch-1 ankyrin domain: Repeats 4 through 7 preserve an ankyrin fold

Olga Y. Lubman, Raphael Kopan, Gabriel Waksman, Sergey Korolev

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Folding and stability of proteins containing ankyrin repeats (ARs) is of great interest because they mediate numerous protein-protein interactions involved in a wide range of regulatory cellular processes. Notch, an ankyrin domain containing protein, signals by converting a transcriptional repression complex into an activation complex. The Notch ANK domain is essential for Notch function and contains seven ARs. Here, we present the 2.2 Å crystal structure of ARs 4-7 from mouse Notch 1 (m1ANK). These C-terminal repeats were resistant to degradation during crystallization, and their secondary and tertiary structures are maintained in the absence of repeats 1-3. The crystallized fragment adopts a typical ankyrin fold including the poorly conserved seventh AR, as seen in the Drosophila Notch ANK domain (dANK). The structural preservation and stability of the C-terminal repeats shed a new light onto the mechanism of heterooligomeric assembly during Notch-mediated transcriptional activation.

Original languageEnglish
Pages (from-to)1274-1281
Number of pages8
JournalProtein Science
Volume14
Issue number5
DOIs
StatePublished - May 2005

Keywords

  • Ankyrin repeats
  • Crystal structure
  • Notch

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