Abstract
Galectin-1 is an important regulator of leukocyte function and tumor angiogenesis. Recently, this lectin has been identified as a molecular target for the potent angiogenesis inhibitor anginex. Here, we report 1H, 13C, and 15N chemical shift assignments for human galectin-1 as determined by using heteronuclear triple resonance NMR spectroscopy.
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Acknowledgments
This work was made possible by a research grant from the National Cancer Institute (CA-096090) to KHM and NIH NRSA training grant (HL 07062) to IVN. NMR instrumentation was provided with funds from the National Science Foundation (BIR-961477), the University of Minnesota Medical School, and the Minnesota Medical Foundation.
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Nesmelova, I.V., Pang, M., Baum, L.G. et al. 1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer. Biomol NMR Assign 2, 203–205 (2008). https://doi.org/10.1007/s12104-008-9121-9
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DOI: https://doi.org/10.1007/s12104-008-9121-9