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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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Publisher copy:
10.1016/j.str.2013.03.012

Authors


Soundararajan, M More by this author
Savitsky, P More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Eswaran, J More by this author
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Journal:
Structure
Volume:
21
Issue:
6
Pages:
986-996
Publication date:
2013-06-04
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:c7344c3b-8900-4129-888a-02e144b052db
Source identifiers:
405855
Local pid:
pubs:405855

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