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1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer
Published Web Location
http://link.springer.com/article/10.1007/s12104-008-9121-9/fulltext.htmlNo data is associated with this publication.
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 (1)H, (13)C, and (15)N chemical shift assignments for human galectin-1 as determined by using heteronuclear triple resonance NMR spectroscopy.
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