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The crystal structure of a partial mouse Notch‐1 ankyrin domain: Repeats 4 through 7 preserve an ankyrin fold
Author(s) -
Lubman Olga Y.,
Kopan Raphael,
Waksman Gabriel,
Korolev Sergey
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.041184105
Subject(s) - ankyrin repeat , ankyrin , microbiology and biotechnology , biology , notch signaling pathway , protein structure , egf like domain , protein folding , protein domain , genetics , biochemistry , gene , signal transduction
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 hetero‐oligomeric assembly during Notch‐mediated transcriptional activation.