view article

Figure 3
Close-up view of the nonreducing end of heparin chain a with Δ4UAp2S. The stereo panels show a close-up view of the centre of the antiparallel (APLP1 E2)2 assembly. Selected amino-acid side chains involved in heparin binding are shown as stick models and are coloured according to the individual protein chains in magenta (chain a) or in cyan (chain b). C atoms of individual heparin chains are coloured likewise. Specific interactions between amino-acid side chains and sugar residues are highlighted with orange dashes. Amino-acid side chains and sugar residues are numbered. (a) The FoFc kicked heparin OMIT electron-density map is contoured at 3.5σ (green mesh). (b) Substitution of Δ4UAp2S by IdoAp2S at the nonreducing end of heparin chain a. Colours are as in (a). The final structure with Δ4UAp2S at the nonreducing end [as shown in (a)] is shown for comparison as a grey-coloured ball-and-stick model. The FoFc kicked heparin OMIT electron-density map is contoured at −4.0σ (red mesh).

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds