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. 2007 Feb 7;1:61–76.

Figure 1a.

Figure 1a

Amino acid sequence in α1(II) chain of human procollagen type IIB (COL2A1_HUMAN, P02458, UniProtKB/Swiss). Numbering of amino acids in this figure (and throughout the whole text of this review) is consistent with numbering in the source given above and may not correspond to numbering in a particular reference. Numbering used here includes N-terminal signal peptide and N-propeptide, and does not include the alternatively spliced block of 69 amino acids in the N-propeptide (which is shown in Figure 1b). Each number corresponds to the last one of ten amino acids under it.

- Tandems Proline/Hydroxyproline and Lysine/Hydroxylysine are not distinguished and are represented by the same letter (P and K, respectively).

- Positions of cross-links are color-coded and underlined (K121, 239, 1061, and 1162).

- The telopeptides (in red lettering) and epitopes discussed in this review is as follows:

113–131 N-terminal non-helical domain (N-terminal telopeptide)

1146–1172 C-terminal non-helical domain (C-terminal telopeptide)

132–1145 Triple-helical domain

1173–1418 Carboxy-terminal propeptide domain

26–112 Amino-terminal propeptide domain