ArticleProtein science : a publication of the Protein Society2007
The pro-peptide of proNGF: structure formation and intramolecular association with NGF.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 33 citations in OpenAlex.
- A combined evolutionary and structural approach to disclose the primary structural determinants essential for proneurotrophins biological functions.Computational and structural biotechnology journal · 2021Article
- Recombinant rabbit beta nerve growth factor production and its biological effects on sperm and ovulation in rabbits.PloS one · 2019Article
- Pro region engineering of nerve growth factor by deep mutational scanning enables a yeast platform for conformational epitope mapping of anti-NGF monoclonal antibodies.Biotechnology and bioengineering · 2018Article
- Conformational characterization of nerve growth factor-β reveals that its regulatory pro-part domain stabilizes three loop regions in its mature part.The Journal of biological chemistry · 2017Article
- HBpF-proBDNF: A New Tool for the Analysis of Pro-Brain Derived Neurotrophic Factor Receptor Signaling and Cell Biology.PloS one · 2016Article
- The conundrum of the high-affinity NGF binding site formation unveiled?Biophysical journal · 2015Article
- Article
- Enhancement of Streptomyces transglutaminase activity and pro-peptide cleavage efficiency by introducing linker peptide in the C-terminus of the pro-peptide.Journal of industrial microbiology & biotechnology · 2013Article
- Conformational plasticity of proNGF.PloS one · 2011Article
- Identification of a linear epitope in sortilin that partakes in pro-neurotrophin binding.The Journal of biological chemistry · 2010Article
- Molecular and structural insight into proNGF engagement of p75NTR and sortilin.Journal of molecular biology · 2010Article
- Proneurotrophins require endocytosis and intracellular proteolysis to induce TrkA activation.The Journal of biological chemistry · 2008Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The pro-peptide of human nerve growth factor (NGF) functions as an intramolecular chaperone during oxidative renaturation of proNGF in vitro and interacts intramolecularly with the mature part of native proNGF. Here, we analyzed the structure formation and stability of the pro-peptide in the context of proNGF and its intramolecular interaction with the native mature part. Folding and unfolding of the NGF-coupled pro-peptide, as analyzed by fluorescence, were biphasic reactions with both phases depending on the interaction with the mature part. This interaction was characterized by an overall stability of DeltaG = 20.9 kJ/mol that was subdivided into two reactions, native <--> intermediate state (14.8 kJ/mol) and intermediate <--> unfolded state (6.1 kJ/mol). An additional very fast unfolding reaction was observed using circular dichroism (CD), indicating the presence of at least two kinetically populated intermediates in the unfolding of proNGF. The part of the pro-peptide involved in the intramolecular association with mature NGF comprised the peptide Trp(-83)-Ala(-63) as determined by H/D exchange experiments. Spectroscopic analyses revealed that on the NGF side, a surface area around Trp(21) interacted with the pro-peptide. Trp(21) also participates in binding to TrkA and p75 receptors. These overlapping binding sites of the pro-peptide and the NGF receptors might explain the previously observed lower affinity of proNGF to its receptors as compared to NGF.
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