1YMP

The Crystal Structure of a Partial Mouse Notch-1 Ankyrin Domain: Repeats 4 Through 7 Preserve an Ankyrin Fold

Summary for 1YMP

• Entry DOI: 10.2210/pdb1ymp/pdb
• Descriptor: Notch 1 protein (2 entities in total)
• Functional Keywords: ankyrin repeats, helix-turn-helix, transcription
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane; Single-pass type I membrane protein (By similarity). Notch 1 intracellular domain: Nucleus (By similarity): Q07008
• Total number of polymer chains: 2
• Total formula weight: 30155.92

Authors

Lubman, O.Y.,Kopan, R.,Waksman, G.,Korolev, S. (deposition date: 2005-01-21, release date: 2005-05-10, Last modification date: 2023-08-23)

Primary citation

Lubman, O.Y.,Kopan, R.,Waksman, G.,Korolev, S.
The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold.
Protein Sci., 14:1274-1281, 2005

PubMed 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 A 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.

PubMed: 15802643
DOI: 10.1110/ps.041184105

Experimental method

X-RAY DIFFRACTION (2.2 Å)