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Figure 1.
FIG. 1. A, minicollagen-1 amino acid sequence and domain
structure. The propeptide sequence is blue, the MCRDs are red,
polyproline sequences are light green, the collagen repeat is
dark green. B, alignment of MCRDs in minicollagen molecules from
different cnidarians and in NOWA. MCol1h, minicollagen-1 Hydra;
MCol2h, minicollagen-2 Hydra (3); MColad, minicollagen Acropora
donei (2); MColac, minicollagen Acropora cervicornis (1);
MColap, minicollagen Acropora palmate (1); N and C, N-,
C-terminal. The sequence of the Cys-rich region of NOWA in Hydra
(NWh) starts with repeat 1 and terminates with repeat 8.
Residues in MCol1hC are numbered starting at the proline
preceding the first cysteine, and the same numbering was used in
the NMR structures. The highly conserved cysteine residues are
marked in red. Proline in position 12, which is conserved with
two exceptions, is marked in purple. The sequence of the
synthesized and investigated peptide is underlined.
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