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NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1 |
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| Authors: | Navratna Vajpai Anne-Kathrin Schott Martin Vogtherr Alexander L. Breeze |
| Affiliation: | 1. Protein Structure and Biophysics, AstraZeneca R&D, Alderley Park, Macclesfield, Cheshire, SK10 4TG, UK 2. Centre of Clinical Research, University of Freiburg Medical Centre, Breisacher Str. 66, 79106, Freiburg, Germany 3. Merck KGaA, Frankfurter Str. 250, 64293, Darmstadt, Germany |
| Abstract: | Members of the fibroblast growth factor receptor tyrosine kinase family (FGFR1–4) play an important role in many signalling cascades. Although tightly regulated, aberrant activity of these enzymes may lead to, or become features of, disease pathologies including cancer. FGFR isoforms have been the subject of drug discovery programmes, with a number of kinase-domain inhibitors in pre-clinical and clinical development. Here, we present the first (83 % complete) backbone resonance assignments of apo-FGFR1 kinase. |
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