 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](be5268fig2mag.jpg)
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Figure 2
Structural features of SmVAL4 and primary-sequence alignment with selected representative CAP proteins. The sequences were aligned with ClustalW2 and the secondary-structural features are illustrated with the coordinates of SmVAL4 and GLIPR2 using ESPript (Gouet et al., 2003  ). The different secondary-structure elements shown are α-helices (large squiggles labeled α), 310-helices (small squiggles labeled η), β-strands (arrows labeled β) and β-turns (labeled TT). Identical residues are shown in white on a red background and conserved residues are highlighted in yellow. The locations of the cysteine residues involved in disulfide bonds are numbered in green and the signature CRISP motifs are identified by red bars. The representative CAP structures are NaASP2 (PDB entry 1u53
), tablysin-15 (PDB entry 3u3n
), GAPR-1 (PDB entry 1smb
), sGLIPR1 (PDB entry 3qnx
) and vCRISP (PDB entry 1rc9
). |
![[Figure 2]](be5268fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
