NAChRDB: Solving the puzzle of structure-function relationships
to clarify the allostery of nicotinic acetylcholine receptors
(nAChRs)

k 2021

NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs)

CHARESHNEU, Aliaksei, Purbaj PANT, Ravi José Tristao RAMOS, David SEHNAL, Tuğrul GÖKBEL et. al.

Základní údaje

Originální název

NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs)

Autoři

CHARESHNEU, Aliaksei, Purbaj PANT, Ravi José Tristao RAMOS, David SEHNAL, Tuğrul GÖKBEL, Crina-Maria IONESCU a Jaroslav KOČA

Vydání

1st Student Conference in Structural Biology, 2021

Další údaje

Typ výsledku

Prezentace na konferencích

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Změněno: 8. 9. 2021 10:38, Aliaksei Chareshneu, Ph.D.

Anotace

V originále

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

Citovat

CHARESHNEU, Aliaksei, Purbaj PANT, Ravi José Tristao RAMOS, David SEHNAL, Tuğrul GÖKBEL, Crina-Maria IONESCU a Jaroslav KOČA. NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs). In 1st Student Conference in Structural Biology. 2021.

@proceedings{1790447,
   author = {Chareshneu, Aliaksei and Pant, Purbaj and Ramos, Ravi José Tristao and Sehnal, David and Gökbel, Tuğrul and Ionescu, CrinaandMaria and Koča, Jaroslav},
   booktitle = {1st Student Conference in Structural Biology},
   title = {NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs)},
   url = {https://cssb.structbio.org/wp-content/uploads/1stSCSB_booklet_fin.pdf},
   year = {2021}
}

TY  - CONF
ID  - 1790447
AU  - Chareshneu, Aliaksei - Pant, Purbaj - Ramos, Ravi José Tristao - Sehnal, David - Gökbel, Tuğrul - Ionescu, Crina-Maria - Koča, Jaroslav
PY  - 2021
TI  - NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs)
UR  - https://cssb.structbio.org/wp-content/uploads/1stSCSB_booklet_fin.pdf
N2  - 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
ER  -

CHARESHNEU, Aliaksei, Purbaj PANT, Ravi José Tristao RAMOS, David SEHNAL, Tuğrul GÖKBEL, Crina-Maria IONESCU a Jaroslav KOČA. NAChRDB: Solving the puzzle of structure-function relationships to clarify the allostery of nicotinic acetylcholine receptors (nAChRs). In \textit{1st Student Conference in Structural Biology}. 2021.

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