1H, 13C and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer

Irina V. Nesmelova, Mabel Pang, Linda G. Baum, Kevin H. Mayo

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)203-205
Number of pages3
JournalBiomolecular NMR Assignments
Volume2
Issue number2
DOIs
StatePublished - Dec 2008

Bibliographical note

Funding Information:
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.

Keywords

  • Carbohydrate
  • Galactose
  • Galectin
  • NMR
  • Protein

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