1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer.
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.
Nesmelova
Irina V
IV
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, 6-155 Jackson Hall, 321 Church Street, Minneapolis, MN 55455, USA.
Pang
Mabel
M
Baum
Linda G
LG
Mayo
Kevin H
KH
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D019281:Dimerization; D037483:Galectin 1 / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D037483:Galectin 1; D009587:Nitrogen Isotopes; D011522:Protons