Backbone assignment of the tyrosine kinase Src catalytic domain in complex with imatinib View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2011-04-27

AUTHORS

Ramón Campos-Olivas, Marco Marenchino, Leonardo Scapozza, Francesco L. Gervasio

ABSTRACT

The Src tyrosine kinase is the paradigm of an oncogenic kinase, and of regulation by intramolecular inhibitory interactions, as well as an important anticancer target due to its roles in cell proliferation and metastasis. The assignment of backbone 1HN, 13Cα, 13CO, and 15N, and sidechain 13Cβ resonances of the catalytic domain of Src (283 residues) in complex with the anticancer drug Imatinib is reported here. Consistent with previous X-ray studies of the same complex, most signals from the activation loop are not detected, indicating that, even in the presence of the drug, it probably adopts highly heterogeneous conformations in intermediate exchange. For the rest of the polypeptide backbone, assignments have been completed for ~88% of residues, with only a few solvent-exposed amides remaining unassigned. More... »

PAGES

221-224

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12104-011-9304-7

DOI

http://dx.doi.org/10.1007/s12104-011-9304-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001933720

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21523440


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