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![[Figure 4]](rr5158fig4mag.jpg)
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Figure 4
ANX1 and ANX2 share a common ectodomain architecture. (a) Ribbon diagrams of ANX1 (left) and ANX2 (right) show a strong degree of structural conservation (r.m.s.d. of ∼0.6 Å comparing 375 corresponding Cα atoms between ANX1 and ANX2) with a similar orientation of their mal-N and mal-C domains (colours are as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) ). The N-glycan structures observed in ANX1 and ANX2 are highlighted in yellow (in bond representation). (b) Structural superposition of the ANX1 (Cα trace, magenta) and ANX2 (blue) ectodomains (right) and a ribbon diagram of the ANX1 ectodomain with Cα atoms coloured according to their crystallographic temperature factors, from blue to red (left). Note that the N- and C-termini as well as several loop structures assembled around the `cleft' region appear to be flexible. (c) The corresponding the1-1 and the1-2 alleles (shown as orange spheres) are mapped into the ANX1 structure. (d) Analytical size-exclusion chromatography reveals that the ANX1 extracellular domain elutes as a monomer (red line), as do the isolated THE1 (black line), HERK1 (blue line) and ANX2 (green line) ectodomains. The void volume (V0) and total volume (Vt) are shown, together with elution volumes for molecular-mass standards (A, thyroglobulin, 669 000 Da; B, ferritin, 440 000 Da; C, aldolase, 158 000 Da; D, conalbumin, 75 000 Da; E, ovalbumin, 44 000 Da; F, carbonic anhydrase, 29 000 Da; G, ribonuclease A, 13 700 Da.). The molecular masses of purified ANX1, THE1 and HERK1 ectodomains analysed by MS-MALDI-TOF are 58, 63 and 53.5 kDa, respectively. An SDS–PAGE analysis of the purified ectodomains is shown alongside. |
![[Figure 4]](rr5158fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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