Figure 1.
FIGURE 1. Crystal structure of the mouse galectin-9
N-terminal CRD. A, ribbon model of the monomeric structure of
the apo form1 of the galectin-9 N-terminal CRD is shown. The
five-stranded (F1–F5) and six-stranded (S1–S6) -sheets
and one short helix (H1) are indicated by the letter-number
code. The carbohydrate binding site is shown by a dotted box. B,
the dimeric structure of the galectin-9 N-terminal CRD is shown.
Two monomers in an asymmetric unit in the apo form1 crystal are
shown in red (chain-A) and green (chain-B), respectively. C,
close up view of the dimer interface. The amino acid residues
involved in the dimer formation are shown in ball-and-stick
model. The carbon, oxygen, nitrogen, and sulfur atoms are shown
in white, red, blue, and yellow spheres, respectively. Hydrogen
bonds are depicted by red dotted lines. D, electrostatic
potential maps of the dimer surfaces of the galectin-9
N-terminal CRD (upper) and galectin-1 CRD (lower) (PDB code:
1GZW). Positive (blue) and negative (red) potentials are mapped
on the van der Waals surfaces in the range –10 k[B]T (red) to
+10 k[B]T (blue), where k[B] is Boltzmann's constant and T is
the absolute temperature. The orientation of the galectin-9
N-terminal CRD dimer is same as Fig. 1B.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
35884-35893)
copyright 2006.
-sheets
and one short helix (H1) are indicated by the letter-number
code. The carbohydrate binding site is shown by a dotted box. B,
the dimeric structure of the galectin-9 N-terminal CRD is shown.
Two monomers in an asymmetric unit in the apo form1 crystal are
shown in red (chain-A) and green (chain-B), respectively. C,
close up view of the dimer interface. The amino acid residues
involved in the dimer formation are shown in ball-and-stick
model. The carbon, oxygen, nitrogen, and sulfur atoms are shown
in white, red, blue, and yellow spheres, respectively. Hydrogen
bonds are depicted by red dotted lines. D, electrostatic
potential maps of the dimer surfaces of the galectin-9
N-terminal CRD (upper) and galectin-1 CRD (lower) (PDB code:
1GZW). Positive (blue) and negative (red) potentials are mapped
on the van der Waals surfaces in the range –10 k[B]T (red) to
+10 k[B]T (blue), where k[B] is Boltzmann's constant and T is
the absolute temperature. The orientation of the galectin-9
N-terminal CRD dimer is same as Fig. 1B.