Fig. 1.

Phylogenetic analysis and domain organization of CSPG-containing proteins. (A) Phylogenetic trees were constructed from aligned CSPG domain-containing regions of each protein by using neighbor-joining (NJ), maximum parsimony (MP), and minimum evolution (ME) methods. (Mm, Mus musculus; Hs, Homo sapiens; Fr, Fugu rubripes; Dm, Drosophila melanogaster; Ce, C. elegans; and Lv, Lytechinus variegatus. Black spots indicate tree nodes with >95% bootstrap support for all three methods, and the gray spot indicates a node supported to 89% by NJ and MP and 60% by ME. The remaining node was not consistently resolved by these methods. Fr.Fras1 and Mm.Cspg5 are incomplete at their N termini (*). The three lightly shaded CSPG domains only partially match the full domains as defined in B. (B) Multiple sequence alignment of CSPG domains with a cadherin of known structure (16) presented by using chroma (33). The line below the alignment shows the consensus structural features of cadherins aligned to the CSPG domains. E indicates β-strand residues. Residues shown to directly interact with chelated Ca²⁺ ions are shaded; red indicates physical–chemical properties that are >60% conserved between cadherins and CSPGs and gray indicates where they are not conserved. The consensus properties are summarized by the symbol – for negative and by the letters p for polar and h for hydrophobic residues.