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Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function.

Abstract:

Recent reports have provided evidence that the beta-hydroxylation of conserved asparaginyl residues in ankyrin repeat domain (ARD) proteins is a common posttranslational modification in animal cells. Here, nuclear magnetic resonance (NMR) and other biophysical techniques are used to study the effect of asparaginyl beta-hydroxylation on the structure and stability of 'consensus' ARD proteins. The NMR analyses support previous work suggesting that a single beta-hydroxylation of asparagine can s...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2009.07.070

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
Journal:
Journal of molecular biology More from this journal
Volume:
392
Issue:
4
Pages:
994-1006
Publication date:
2009-10-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836

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