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Fig. 8. Missense mutations in the b loop of the first and fourth LE domains abolish the usherin/collagen interaction. (A) Purified type IV collagen and recombinant human usherin (1 µg of each) were mixed with varying relative molar excess amounts of LE domain fusion peptide. Following incubation, complexes were immunoprecipitated with anti-collagen (IV) antibodies, and the immunoprecipitated material digested with collagenase. Remaining material was fractionated by PAGE, and stained with Coomassie Blue. (B) (Left) The three-dimensional structure of a single LE module, based on the mouse laminin 
chain crystal structure. Substituted amino acid residues that obliterate type IV collagen binding activity are shown in red, and residues that did not affect binding are in green. (Right) Location of missense mutations in the LE repeats of usherin. Mutations that abolish collagen binding are in red; mutations that do not affect collagen binding are in green. Mutations in black were not tested.
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