Volume 7 issue 12 December 2006
Novel Binding Sites on Clathrin and Adaptors Regulate Distinct Aspects of Coat Assembly
Christine Knuehl, Chih-Ying Chen, Venus Manalo, Peter K. Hwang, Nobuyuki Ota and Frances M. Brodsky

Legends to Supplementary Figures

Figure S1 . Comparison of the alignments of CHCR1 and CHCR2 with previously published alignment. The top line indicates predicted positions of helices and loops relative to the structure of CHCR6 and CHCR7 (Ybe et al., 1999 (12)). “A” and “a” are helices and dashes are loops. The second line indicates the previously published alignment from (12), used by Fotin et al., 2004 (9) for backbone placement. The third line indicates the new alignment predicted by ClustalX, shown in Figure S2. The fourth line is the alignment of CHCR6 and 7 from (12). Residue numbers at top refer to CHCR1/CHCR2; bottom numbers refer to CHCR6/CHCR7.

Figure S2. Alignment of 63 CHCRs from nine species of CHC. Sequences of CHCRs are listed in order of their similarity to bovine CHCR6, according to alignment by ClustalX (http://www.csc.fi/molbio/progs/clustalw/). The secondary structure assignments, erived from homology modeling and the CHCR6 crystal structure (12), are indicated above the alignment. “A” and “a” are helices and dashes are loops. The annotation on the left indicates species and clathrin repeat (c1 to c7). Colors indicate amino acid conservation at each position: blue, hydrophobic residues; green, serine and threonine; magenta, negatively charged; orange, positively charged; olive, glycine; yellow, proline; purple, histidine. The sequences used for alignment are from the compilation by Wakeham et al., 2005 (15) .

Figure S1 and S2 (.pdf)