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. 1998 Jun 29;141(7):1539–1550. doi: 10.1083/jcb.141.7.1539

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Structures of mouse claudin-1 and -2. (a) Comparison of amino acid sequences of mouse claudin-1 and -2 by the GENETYX program. Identity and homology are indicated by asterisks and dots, respectively. They showed 38% identity at the amino acid sequence level. (b) Hydrophilicity plots for claudin-1 and -2 prepared using the Kyte and Doolittle algorithm. The plot records the average hydrophilicity along the sequence over a window of eight residues. Hydrophilic and hydrophobic residues are in the lower and upper parts of the frames, respectively. The axes are numbered in amino acid residues. Both claudin-1 and -2 appeared to contain four major hydrophobic, potentially membrane-spanning regions (arrows), although the possibility was not excluded that five transmembrane domains were included in these molecules only from these plots as discussed in the text.

Structures of mouse claudin-1 and -2. (a) Comparison of amino acid sequences of mouse claudin-1 and -2 by the GENETYX program. Identity and homology are indicated by asterisks and dots, respectively. They showed 38% identity at the amino acid sequence level. (b) Hydrophilicity plots for claudin-1 and -2 prepared using the Kyte and Doolittle algorithm. The plot records the average hydrophilicity along the sequence over a window of eight residues. Hydrophilic and hydrophobic residues are in the lower and upper parts of the frames, respectively. The axes are numbered in amino acid residues. Both claudin-1 and -2 appeared to contain four major hydrophobic, potentially membrane-spanning regions (arrows), although the possibility was not excluded that five transmembrane domains were included in these molecules only from these plots as discussed in the text.