Fig. 5.
Fig. 5. Structural analysis of the Leu262Proβ3mutation. / (A) Leucine (Leu) 262 is completely conserved among β subunits. The amino acid sequence of human β3 residues cystine (Cys) 232 to Cys273 is shown aligned with frog (Xenopus) and mouse β3 and with the sequences of 7 other human β subunits. Notably, the Leu residue at position 262 (in boldface) is invariant. The proposed intramolecular disulfide loop Cys232-27330is shown. (B) Predicted hydrophobicity and secondary structure are shown for β3 amino acids 200 to 300 containing either wild-type Leu262 (black line) or mutant Pro262 (stippled line with arrow). The position of amino acid 262 is indicated by the vertical line.

Structural analysis of the Leu262Proβ3mutation.

(A) Leucine (Leu) 262 is completely conserved among β subunits. The amino acid sequence of human β3 residues cystine (Cys) 232 to Cys273 is shown aligned with frog (Xenopus) and mouse β3 and with the sequences of 7 other human β subunits. Notably, the Leu residue at position 262 (in boldface) is invariant. The proposed intramolecular disulfide loop Cys232-27330is shown. (B) Predicted hydrophobicity and secondary structure are shown for β3 amino acids 200 to 300 containing either wild-type Leu262 (black line) or mutant Pro262 (stippled line with arrow). The position of amino acid 262 is indicated by the vertical line.

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