Article
Structural studies of receptor binding by cholera toxin mutants.
Protein science : a publication of the Protein Society - 1 Jul 1997
Merritt E A, Sarfaty S, Jobling M G, Chang T, Holmes R K, Hirst T R, Hol W G
Abstract excerpt
The wide range of receptor binding affinities reported to result from mutations at residue Gly 33 of the cholera toxin B-pentamer (CTB) has been most puzzling. For instance, introduction of an aspartate at this position abolishes receptor binding, whereas substitution by arginine retains receptor affinity despite the larger side chain. We now report the structure determination and 2.3-A refinement of the CTB...
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