- Alignment of chitinase-like (glycoside
hydrolase family 18) domains in human and mouse proteins. Regions of secondary structure are
indicated above the alignment and coloured to correspond with the
structure of Ym1, left. Alpha helices in the TIM-like domain (a1-8)
and the small alpha/beta domain (aC) are higlighted in
red.
Beta sheets in the TIM-like domain (b1-8) are highlighted in
blue and those in the
small alpha/beta domain (bA-B, bD-F) in
yellow.
- 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. Cysteine residues which form disulfide bonds are
highlighted in yellow.
with disulfide pairings numbered 1 and 2. Residues from the active site motif DXXDXDXE, which includes the catalytic
glutamate residue, are highlighted in
magenta where identical to
the motif and in pink where
similar.
- Side chains in human YKL-40 which make
hydrogen bonds to bound chito-oligosaccharides, and the conserved
equivalents in other proteins, are highlighted in
red. Hydrophobic
residue of the substrate binding cleft, and the conserved equivalents in
other proteins, are highlighted in
orange. Residues making both hydrogen bonds and hydrophobic
interactions are marked x. Conservation of hydrophobic
residues in YKL-40 and active chitinases, but not in Ym1, may account for
differences in ligand binding specificity.
-
- Accession numbers
- HS = human MM = mouse
-