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Journal article

Structures of Down syndrome kinases, DYRKs, reveal mechanisms of kinase activation and substrate recognition.

Abstract:

Dual-specificity tyrosine-(Y)-phosphorylation-regulated kinases (DYRKs) play key roles in brain development, regulation of splicing, and apoptosis, and are potential drug targets for neurodegenerative diseases and cancer. We present crystal structures of one representative member of each DYRK subfamily: DYRK1A with an ATP-mimetic inhibitor and consensus peptide, and DYRK2 including NAPA and DH (DYRK homology) box regions. The current activation model suggests that DYRKs are Ser/Thr kinases th...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2013.03.012

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
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Journal:
Structure (London, England : 1993)
Volume:
21
Issue:
6
Pages:
986-996
Publication date:
2013-06-01
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
Source identifiers:
401241
Language:
English
Keywords:
Pubs id:
pubs:401241
UUID:
uuid:a0b14ad4-73d5-4078-b6b8-7fcc3ee6bba4
Local pid:
pubs:401241
Deposit date:
2013-11-16

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