Ficolins - sequence alignment
- Alignment of ficolin and horseshoe crab tachylectin fibrinogen-like domains. The extreme N-termini of the domains are omitted due to low similarity. Regions of secondary structure are indicated above the alignment and coloured to correspond with the structure of TL-5A, left. Beta-sheets are labelled b2-b12 and highlighted in blue, alpha-helices are labelled a3-a9 and highlighted in red. Residues that are identical in over 75% of the aligned sequences are highlighted in green. Residues that are similar in over 75% of the sequences are highlighted in cyan. Residues which are less well conserved but are implicated in sugar binding by the structure of TL-5A (left) are highlighted in light green. Conserved cysteine residues which are involved in disulphide bonds are highlighted in yellow. Residues in the TL-5A crystal structure which make contacts with GlcNAc are indicated by S. Residues which coordinate the calcium ion are indicated by C. At the non-conserved positions marked C, it is the main chain which coordinates the calcium ion. The sequence of human fibrinogen beta is aligned beneath the ficolin sequences; [....] indicates insertions in fibrinogen that are not present in ficolins.
- Accession numbers
- Gallus gallus (GG) Ficolin 2 XP_415571
- NB The numbering of proteins as ficolin 1, ficolin 2 etc in different species does not imply an orthologous relationship between these proteins.
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Structure of TL-5A CRD with bound GlcNAc
GlcNAc and Ca2+ are shown in dark blue. Protein Data Bank structure ID: 1JC9.
