Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin
Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin
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Publisher
Chichester, UK: John Wiley & Sons, Ltd
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Language
English
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Publisher
Chichester, UK: John Wiley & Sons, Ltd
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Contents
Protein phosphorylation represents a ubiquitous control mechanism in living cells. The structural prerequisites and consequences of this important post‐translational modification, however, are poorly understood. Oncoprotein 18/stathmin (Op18) is a globally disordered phosphoprotein that is involved in the regulation of the microtubule (MT) filament...
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Full title
Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin
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Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1083899
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1083899
Other Identifiers
ISSN
1469-221X
E-ISSN
1469-3178
DOI
10.1093/embo-reports/kve105