p(HGNC:CHRNA7, var("p.Trp55Ala"))
There is evidence that ApoE directly interacts with nAChRs. An APOE-derived peptide blocks nAChRs on rat hippocampal slices with a submicromolar affinity, and this action is dependent on an arginine-rich segment of the APOE peptide (Klein and Yakel, 2004). Block of heterologously expressed alpha7 nAChRs is greater than that for alpha4beta2 or alpha2beta2 nAChRs (Gay et al., 2006). This block of alpha7 receptors is abolished when alpha7 Trp55 is mutated to alanine, providing strong evidence that it results from a direct interaction between the peptide and the receptors (Gay et al., 2007), and the effects of other substitutions of Trp55 suggests that this interaction is hydrophobic PubMed:19293145
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.