Crystal structure of the catalytic domain of human atypical protein kinase 
C-iota reveals interaction mode of phosphorylation site in turn motif

Messerschmidt, A.; Macieira, Sofia; Velarde, Milko; Badeker, M.; Benda, C.; Jestel, A.; Brandstetter, H.; Neuefeind, T.; Blaesse, M.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif

MPS-Authors

/persons/resource/persons78394

Messerschmidt, A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78347

Macieira, Sofia
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78826

Velarde, Milko
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Messerschmidt, A., Macieira, S., Velarde, M., Badeker, M., Benda, C., Jestel, A., et al. (2005). Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. Journal of Molecular Biology, 352(4), 918-931.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6576-A

Abstract

There is no abstract available