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NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1

NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1

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Publisher
Springer Journals
Copyright
Copyright © 2013 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-013-9458-6
pmid
23325512
Publisher site
See Article on Publisher Site

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.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jan 17, 2013

References