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Table 1 Characteristics of single nucleotide variants (SNVs) located in the N-terminal domain of nAChR hα6 subunit

From: Analysis of rare variations reveals roles of amino acid residues in the N-terminal extracellular domain of nicotinic acetylcholine receptor (nAChR) alpha6 subunit in the functional expression of human alpha6*-nAChRs

rs ID # Nucleotide position in chromosome 8 All [AA + EA] Allele # Amino acid change Change in electrical charge Conservation in human nAChR α subunits Conservation in α6 subunits of other species NTD location
rs140930963 8:42620300 G = 37/A = 10721 S43P   No -   α-helix
rs80342906 8:42620289 C = 6/G = 10752 N46K   No N: yes   α-helix
rs149966755 8:42620258 T = 1/C = 10757 D57N ‘-‘ve to zero D: weak D: yes   α-helix
unknown 8:42614217 A = 2/G = 10756 R87C ‘+’ve to zero R: strong R: yes Complementary face/inner β-sheet Strand β2
rs146332801 8:42612169 C = 1/A = 10755 D92E   D: fully D: yes β2-β3 loop (loop D)
rs188620180 8:42612158 A/G R96H   No - β2-β3 loop
rs200380236 8:42612144 T = 1/C = 10755 E101K ‘-‘ve to ‘+’ve No E: yes β2-β3 loop/1MIR
unknown 8:42611874 C = 1/A = 10757 S156R neutral to ‘+’ve S: fully S: yes Strand β6
unknown 8:42611747 A = 2/C = 10756 D199Y ‘-’ve to neutral D: weak D: weak β8-β9 loop (loop F)
rs143385261 8:42611734 G = 3/T = 10755 N203T   N: weak N: weak   β8-β9 loop (loop F)
rs141518931 8:42612110 A = 1/G = 10755 A112V   No A: yes Principal face/outer β-sheet β3-β4 loop (Loop A)
rs79945499 8:42611829 G/C N171K neutral to ‘+’ve N: strong N: yes β6-β7 (Cysteine loop)
rs200745568 8:42611791 T = 1/G = 10757 A184D neutral to ‘-‘ve No A: yes β7-β8 loop (loop B)
rs199987912 8:42611665 G = 2/A = 10756 I226T   No I: yes β9-β10 loop (loop C)
unknown 8:42611644 C = 1/G = 10757 S233C   No S: yes   Strand β10
  1. 1MIR: Main immunogenic region.
  2. Pertinent information about the N-terminal variations in nAChR hα6 subunit such as their reference SNP (rs) identification (ID) number, location in the chromosome 8, combined frequency of nucleotide variations discovered in more than 10000 genomes of African Americans (AA) and European Americans (EA) (Exome Sequencing Project: ESP; https://esp.gs.washington.edu/), change in amino acids, change in electrical charges, conservation in the human nAChR α subunits (Figure 1), conservation in nAChR α6 subunit of other species and putative locations in the secondary structure of the nAChR hα6 subunits (Figure 2) are presented. The WT AAs with the exception of S43 are strongly conserved in nAChR α6 subunits studied from a limited number of other species (Figure 1). Please note that hα6 variations R87C, S156R, D199Y and S233C retrieved from ESP do not have an rs ID number yet. The N-terminal domain of a typical human nAChR subunit is presumed to contain an inner β-sheet (strand β1-β3, β5, β6 and β8) and outer β-sheet (strand β4, β7, β9 and β10) like those of seen in the crystal structure of Torpedo muscle nAChR subunits. ‘-‘ indicates lack of indicated information in these positions.