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![[Figure 1]](rr5158fig1mag.jpg)
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Figure 1
Architecture of the tandem malectin-like ectodomain of ANX1. (a) Front and 180° rotated views of the ANX1 ectodomain (ribbon diagram) with mal-N (residues 26–187) shown in magenta, the β-hairpin in orange and mal-C (residues 210–411) in blue. (b) Structural superposition of the ANX1 mal-N domain (Cα trace; magenta) onto mal-C (blue). The r.m.s.d. is ∼2 Å comparing 127 corresponding Cα atoms. (c, d) Structural superpositions of the ANX1 mal-N domain (magenta) onto (c) the animal malectin from X. laevis (light blue; PDB entry 2k46; Schallus et al., 2008  ) and (d) the bacterial carbohydrate-binding module (CBM22) from Paenibacillus barcinonensis (grey; PDB entry 4xur; Sainz-Polo et al., 2015). The r.m.s.d.s are ∼2.2 Å comparing 127 corresponding Cα atoms and ∼3.1 Å comparing 119 corresponding Cα atoms, respectively. |
![[Figure 1]](rr5158fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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