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. 2015 May 20;71(Pt 6):643–649. doi: 10.1107/S2053230X1500271X

Figure 2.

Figure 2

Structural relationships among ASPs. Structure-based alignment of HPI with Na-ASP-2 from N. americanus (PDB entry 1u53; Asojo et al., 2005 ▶), Ac-ASP-7 from A. caninum (second domain, PDB entry 3nt8; Asojo, 2011 ▶) and Oo-ASP-1 from Ostertagia ostertagi (PDB entry 4g2u; Borloo et al., 2013 ▶). The CAP1–CAP4 motifs are highlighted in green. Conserved disulfide bonds 1–5 are highlighted in black. The two histidine positions found in the ‘active-site’ cleft are marked by hash marks and the candidate disintegrin motifs are marked by asterisks. The consensus sequences for CAP1–CAP4 in PROSITE nomenclature are as follows: CAP1, [GDER][HR][FYWH][TVS][QA][LIVM][LIVMA]Wxx[STN]; CAP2, [LIVMFYH][LIVMFY]XC[NQRHS]Yx[PARH]x[GL]N[LIVMFYWDN]; CAP3, HNxxR; CAP4 G[EQ]N[ILV] (Gibbs et al., 2008 ▶).