Spatial Structure and Activity of Synthetic Fragments of Lynx1 and of Nicotinic Receptor Loop C Models.
Adaptor Proteins, Signal Transducing
/ chemistry
Animals
Bacterial Proteins
/ chemistry
Binding Sites
Bungarotoxins
/ chemistry
Carrier Proteins
/ chemistry
Humans
Ligands
Lymnaea
/ chemistry
Models, Molecular
Neurotoxins
/ chemistry
Peptides
/ chemistry
Protein Binding
/ genetics
Protein Conformation, beta-Strand
Receptors, Nicotinic
/ chemistry
circular dichroism
nicotinic acetylcholine receptors
nuclear magnetic resonance
peptide fragments
radioligand assay
spatial structure
three-finger proteins
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
22 12 2020
22 12 2020
Historique:
received:
08
10
2020
revised:
06
12
2020
accepted:
19
12
2020
entrez:
30
12
2020
pubmed:
31
12
2020
medline:
24
6
2021
Statut:
epublish
Résumé
Lynx1, membrane-bound protein co-localized with the nicotinic acetylcholine receptors (nAChRs) and regulates their function, is a three-finger protein (TFP) made of three β-structural loops, similarly to snake venom α-neurotoxin TFPs. Since the central loop II of α-neurotoxins is involved in binding to nAChRs, we have recently synthesized the fragments of Lynx1 central loop, including those with the disulfide between Cys residues introduced at N- and C-termini, some of them inhibiting muscle-type nAChR similarly to the whole-size water-soluble Lynx1 (ws-Lynx1). Literature shows that the main fragment interacting with TFPs is the C-loop of both nAChRs and acetylcholine binding proteins (AChBPs) while some ligand-binding capacity is preserved by analogs of this loop, for example, by high-affinity peptide HAP. Here we analyzed the structural organization of these peptide models of ligands and receptors and its role in binding. Thus, fragments of Lynx1 loop II, loop C from the
Identifiants
pubmed: 33374963
pii: biom11010001
doi: 10.3390/biom11010001
pmc: PMC7821949
pii:
doi:
Substances chimiques
AChBP protein, Lymnaea
0
Adaptor Proteins, Signal Transducing
0
Bacterial Proteins
0
Bungarotoxins
0
Carrier Proteins
0
LYNX1 protein, human
0
Ligands
0
Neurotoxins
0
Peptides
0
Receptors, Nicotinic
0
hook protein, bacterial flagellum
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 16-14-00215p
Pays : International
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