 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](rf5050fig1mag.jpg)
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Figure 1
Cysteine conservation within the S100 family. (a) Sequence alignment of the 36 distinct representative S100 protein sequences. Human proteins were chosen as representative of mammalian/bird S100 proteins and zebrafish (Danio rerio) proteins for teleost/amphibian/reptile S100 proteins, except for S100Q and S100R which are from Dichotomyctere nigoviridis. The secondary-structure elements classically found in the S100 fold are shown above the alignment. Cysteine residues are boxed in green and the hotspot position for cysteine conservation (84) is highlighted with a green frame. (b) Percentage of sequences retrieved after protein BLAST on each unique sequence displayed in (a) that contain a cysteine in helix H4 and/or at position 84. |
![[Figure 1]](rf5050fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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