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NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs)
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Rok publikování | 2021 |
Druh | Další prezentace na konferencích |
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Popis | Nicotinic acetylcholine receptor (nAChR) is an evolutionary ancient allosteric membrane protein mediating synaptic transmission [1]. These prototypic pentameric ligand-gated ion channels (pLGICs) are expressed in many tissues & species, being involved in neuromuscular transmission, cognition, energy metabolism, and many pathologies (snake envenomation, myasthenia gravis, Parkinson & Alzheimer diseases, addictions, possibly COVID-19 [2]). Since nAChR isolation in 1970 [3], extensive studies resulted in ~5000 publications with huge amounts of structural-functional data. However, the cumulative residue-level knowledge on nAChRs is not systematically accessible. Scatteredness of literature data, aliases & diverse terminology, various receptor types & residue numbering schemes make it harder to summarize the current knowledge and apply it efficiently to promote the further discoveries. There is no single resource providing access to & visualization of such vast information. NAChRDB [4] (https://crocodile.ncbr.muni.cz/Apps/NAChRDB/) fills this gap by: a) delivering relevant & systematized structural-functional residue-level information collected from the literature and b) facilitating its interpretation via mapping onto interactive 3D visualization & sequence alignment. In addition, literature data is supplemented by the computational predictions of potentially allosterically important residues based on the charge profile analysis. Figure 1. NAChRDB workspace. By providing quick & easy access to the structural-functional knowledge via a user-friendly interface (Fig. 1), accompanied by interactive tutorials and case studies, NAChRDB can both serve as an educational resource and a practical tool, helping to study allosteric regulation, reveal gaps in the current knowledge, and guide the further studies in the fields of nAChRs and pLGICs |