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.

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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, 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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-6576-A Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-6578-6

Genre: Journal Article

Alternative Title : J. Mol. Biol.

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Creators:
Messerschmidt, A.¹, Author
Macieira, Sofia¹, Author
Velarde, Milko¹, Author
Badeker, M., Author
Benda, C.², Author
Jestel, A., Author
Brandstetter, H.², Author
Neuefeind, T., Author
Blaesse, M., Author

Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155
2External Organizations, ou_persistent22

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Free keywords: AGC protein kinase; bis(indolyl)maleimide 1 inhibitor; atypical protein kinase C; turn motif phosphorylation; X-ray structure

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Language(s): eng - English

Dates: Date issued: 2005-09-30

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 256273
ISI: 000232188100012

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Title: Journal of Molecular Biology

Alternative Title : J. Mol. Biol.

Source Genre: Journal

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Pages: - Volume / Issue: 352 (4) Sequence Number: - Start / End Page: 918 - 931 Identifier: ISSN: 0022-2836