Figure 1
Crystal structure of human V-1 in the apo form. (a) Overall structure of human V-1 in the asymmetric unit. The whole of chain A is shown in cyan. Helix–turn–helix regions and loop regions of chain B are shown in green and orange, respectively. The N- and C-termini of each chain are indicated. Cys2 residues are shown as spheres. (b) Close-up view of the S—S bond formed at the noncrystallographic dimer interface. (c) Size-exclusion column chromatography. Human V-1 was run through a Superdex 200 10/300 size-exclusion column equilibrated with PBS supplemented with 1 mM DTT. Protein elution was monitored by the absorbance at 280 nm. The elution positions of size markers, namely ribonuclease A (molecular weight 13 700), carbonic anhydrase (molecular weight 29 000) and ovalbumin (molecular weight 43 000), are indicated by arrows. |