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Mutation of tryptophan-21 in mouse nerve growth factor (NGF) affects binding to the fast NGF receptor but not induction of neurites on PC12 cells.

作者信息

Drinkwater C C, Suter U, Angst C, Shooter E M

机构信息

Department of Neurobiology, Stanford University School of Medicine, California 94305-5401.

出版信息

Proc Biol Sci. 1991 Dec 23;246(1317):307-13. doi: 10.1098/rspb.1991.0159.

DOI:10.1098/rspb.1991.0159
PMID:1686097
Abstract

By using in vitro DNA mutagenesis, we replaced the tryptophan residue at position 21 in mouse nerve growth factor (NGF) with either phenylalanine, leucine or serine. Yield, biological activity, immunological reactivity and receptor binding of the recombinant proteins were determined. All three mutants were produced at considerably lower yields than wild-type NGF, with the serine mutant being undetectable. The results of competitive binding assays show that tryptophan-21 is involved in recognition of the fast NGF receptor of PC12 cells. However, specific biological activity of NGF is not altered by the replacement of tryptophan-21. Our results therefore suggest that biological activity of NGF is not directly coupled to binding to the fast NGF receptor.

摘要

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