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1ymp

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(New page: 200px<br /><applet load="1ymp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ymp, resolution 2.200&Aring;" /> '''The Crystal Structu...)
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caption="1ymp, resolution 2.200&Aring;" />
caption="1ymp, resolution 2.200&Aring;" />
'''The Crystal Structure of a Partial Mouse Notch-1 Ankyrin Domain: Repeats 4 Through 7 Preserve an Ankyrin Fold'''<br />
'''The Crystal Structure of a Partial Mouse Notch-1 Ankyrin Domain: Repeats 4 Through 7 Preserve an Ankyrin Fold'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1YMP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YMP OCA].
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1YMP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMP OCA].
==Reference==
==Reference==
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[[Category: Kopan, R.]]
[[Category: Kopan, R.]]
[[Category: Korolev, S.]]
[[Category: Korolev, S.]]
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[[Category: Lubman, O.Y.]]
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[[Category: Lubman, O Y.]]
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
[[Category: ankyrin repeats]]
[[Category: ankyrin repeats]]
[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:53 2008''

Revision as of 14:06, 21 February 2008


1ymp, resolution 2.200Å

Drag the structure with the mouse to rotate

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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