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Structural conservation of CAP-GLY domains
Structure and conservation of the CAP-GLY motif. A, B: X-ray structures of the CAP-GLY motifs of proteins tubulin folding cofactor B (A,1TOV) and dynactin p150 (B,1TXQ) as obtained from the PDB. The striking similarity between these proteins suggests that the CAP-GLY motifs of CLIP-170 and its orthologs will have similar structures. C: Conservation of the CAP-GLY motifs of fungal bik1 homologs mapped onto the p150 structure shown in ribbon (left) or spacefill (right) format. Amino acids identical in at least 80% of sequences are colored dark red, those similar in at least 80% are colored red. All positions not matching either of these criteria are colored yellow, with the exception of the the highly conserved GKNDG motif , which is colored purple for orientation purposes. The numbers of selected S. cerevisiae bik1 residues are also given; those in black are different from the p150 residues shown. The orientation of all structures is the same (the addition of side chains changes the appearance of the structure greatly). Rendering and conservation mapping were performed with Protein Explorer (http://molvis.sdsc.edu/protexpl/).
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