Mutation of Asn128 to Asp of Phaseolus vulgaris leucoagglutinin (PHA-L) eliminates carbohydrate-binding and biological activity |
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Authors: | Mirkov TErik; Chrispeels Maarten J |
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Institution: | Department of Biology and Center for Molecular Genetics, University of California San Diego, La Jolla, CA 92093-0116, USA |
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Abstract: | Phytohaemagglutinin (PHA) is the major lectin present in theseeds of the common bean, Phaseolus vulgaris, and PHA-L is theleucocyte-agglutinating form of this lectin. This tetramericglycoprotein accumulates in the vacuoles of storage parenchymacells. Based on amino acid sequence comparisons of legume lectinsand the three-dimensional structure of lectin-carbohydrate complexes,Asn128 can be identified as a likely candidate for site-directedmutagenesis to create a mutant PHA-L that does not bind carbohydrate.PHA-L N128 |
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