Conservation and variable sites of amino acids in alpha-subunits of nicotine acetylcholine receptors and alpha-bungarotoxin-binding proteins

Kostetskii, P.V.; Arkhipova, S.F.; Utkin, Y.N.; Tsetlin, V.I.

Biokhimiya 59(2): 206-214


Accession: 008376879

Download citation:  

Article/Abstract emailed within 1 workday
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

A comparative study has been carried out of homologous amino acid sequences of alpha-subunits of acetylcholine receptors (AChR) and related proteins classified into three groups: (i) alpha-bungarotoxin-binding alpha-subunits of nicotine AChR from vertebrate muscles and electrical organ of the skate; (ii) alpha-bungarotoxin-binding alpha-subunits of neuronal AChR from chicken and rat brain and (iii) alpha-bungarotoxin-binding alpha-subunit of chicken brain proteins. The experimental results were plotted as intergroup variability profiles obtained by comparison of all the sequences within one group with each of the sequences in the other group. All of the local variability profiles appeared to be similar and contained both highly conservative and highly variable sites. To the former one may relate the transmembrane segments M1, M3 and, particularly, M2 as well as the 81-100 domain comprising several links pertaining to the ligand-binding domain in AChR. Domains 153-171 and 177-197 comprising most of the identified links involved in the binding of low molecular weight agonists and of alpha-bungarotoxin appeared to be highly variable ones.