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PDBsum entry 1ymp
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Transcription
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PDB id
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1ymp
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References listed in PDB file
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Key reference
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Title
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The crystal structure of a partial mouse notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold.
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Authors
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O.Y.Lubman,
R.Kopan,
G.Waksman,
S.Korolev.
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Ref.
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Protein Sci, 2005,
14,
1274-1281.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. (A) Simplified schematic diagram of the
Notch-mediated transcriptional "switch." NICD is composed of a
membrane proximal RAM domain (yellow), seven ARs (red), and
C-terminal PEST, OPA domains (navy). Binding of NICD to CSL
displaces transcriptional repressors (SMRT, HDAC, CIR) and leads
to recruitment of transcriptional activators MAM and HAT. (B) A
2.2 Å crystal structure of mouse Notch1 ARs 3  -7. There are
two molecules in the asymmetric unit of the crystal. Repeats 3
-7 of molecule
A are colored red, yellow, green, brown, and cyan, respectively.
Repeats of molecule B are colored gray. (C) Structural overlay
of partial ANK domain of mouse Notch-1 with ARs is color coded
as in B and the dANK domain of the Drosophila Notch receptor is
shown in a gray transparent worm representation.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2005,
14,
1274-1281)
copyright 2005.
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