1ymp
From Proteopedia
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The Crystal Structure of a Partial Mouse Notch-1 Ankyrin Domain: Repeats 4 Through 7 Preserve an Ankyrin Fold
Overview
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.
About this Structure
1YMP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold., Lubman OY, Kopan R, Waksman G, Korolev S, Protein Sci. 2005 May;14(5):1274-81. Epub 2005 Mar 31. PMID:15802643
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