ArticleProtein science : a publication of the Protein Society1996
Mutational studies of conserved residues in the dimer interface of nerve growth factor.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 13 citations in OpenAlex.
- Monoclonal antibodies against nitrated nerve growth factor reveal an oxidation-dependent pathogenic hallmark in ALS.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Identification of amino acid residues of nerve growth factor important for neurite outgrowth in human dorsal root ganglion neurons.The European journal of neuroscience · 2019Article
- Molecular dynamics simulations of the NGF-TrkA domain 5 complex and comparison with biological data.Biophysical journal · 2003Article
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5 authors at 1 institution in 1 country.
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Abstract
An understanding of the structure-function relationship of nerve growth factor (NGF) requires precise knowledge of all the residues and regions that participate in NGF receptor binding, receptor activation, and biological activity. Seven recombinant human NGF mutants having alanine substituted for residues located either in the NGF dimer interface or beta-strand region were studied to determine the role of each amino acid residue in NGF biological activity. F86A, T91A, R100A, and R103A remained nearly full active with 61, 120, 91, and 73% of wild-type activity, respectively, in the PC12 cell bioassay. Hydrophobic core and dimer interface residues Y52, F53, and F54 were studied in more detail. Y52A and F54A were expressed in very low levels, suggesting that these two residues may be important for protein stability. Y52A retained full biological activity (91%). F53A had a 20- and 70-fold reduction in biological activity and TrkA phosphorylation, respectively, with only a 5- to 10-fold effect on TrkA binding and no effect on low-affinity receptor binding. F54A had significantly decreased TrkA phosphorylation and biological activity (40-fold). The results suggest that F53 and F54 may play a structural role in TrkA receptor activation subsequent to binding.
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