journal menu
![[Figure 2]](rr5158fig2mag.jpg)
|
|
Figure 2
The malectin-like domains of ANX1 are structurally stabilized by calcium ions. (a) Ribbon diagram of the ANX1 ectodomain coloured as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) and including the positions of two stabilizing calcium ions (black spheres). (b) Details of the ANX1 mal-N (magenta) and mal-C (cyan) calcium ion-binding sites. Residues are in bond representation and metal-coordinating interactions are indicated by solid lines. (c) The ANX1 calcium-ion positions map to structural and not enzymatic calcium-binding sites in CBMs. Structural superposition of the ANX1 mal-N domain (ribbon diagram, in magenta) with the CBM35 bound to digalacturonic acid (PDB entry 2vzq; the r.m.s.d. is ∼3.7 Å comparing 68 corresponding Cα atoms; Montanier et al., 2009) shown in grey. CBM35 contains two calcium ions, depicted as black spheres: one is in the catalytic binding site in close proximity to the carbohydrate and the other has a structural role and is located on the opposite face of the binding groove. The position of the latter site corresponds to the observed calcium-binding site in ANX1 (shown as a magenta sphere). |
![[Figure 2]](rr5158fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
