Table 1.
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 |
1MIR: Main immunogenic region.
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.