C-DOMAIN strands, turns and loops | IMGT positions | Homo sapiens IGHG1 | Homo sapiens IGKC | Homo sapiens IGLC1 | ||
---|---|---|---|---|---|---|
CH1 | CH2 | CH3 | ||||
A-STRAND | 1.5-15 | K1.1 | ||||
K1.2 | ||||||
K10 | ||||||
K12 | K12 | |||||
K15 | ||||||
B-STRAND | 16-26 | K16 | ||||
K18 | ||||||
C23 | C23 | C23 | C23 | C23 | ||
K26 | ||||||
BC-LOOP | 27-38 | K38 | K38 | |||
C-STRAND | 39-45 | W41 | W41 | W41 | W41 | W41 |
K42 | K42 | |||||
CD-STRAND | 45.1-45.5 | K45.4 | ||||
D-STRAND | 77-84 | K79 | K79 | |||
K81 | ||||||
K82 | ||||||
DE-TURN | 84.1-85.1 | K84.1 | ||||
N84.4 | K84.4 | |||||
K85.3 | ||||||
E-STRAND | 85-93 | K88 | ||||
V89 | L89 | L89 | L89 | L89 | ||
K93 | K93 | |||||
F-STRAND | 97-104 | K97 | ||||
K98 | ||||||
K100 | K100 | |||||
K103 | ||||||
C104 | C104 | C104 | C104 | C104 | ||
FG-LOOP | 105-117 | K105 | ||||
K109 | K109 | |||||
K116 | ||||||
G-STRAND | 118-127 | D118 | E118 | Q118 | T118 | E118 |
K119 | K119 | K119 | K119 | K119 | ||
K120 | ||||||
K123 | ||||||
K125 | ||||||
CHS | K130 | |||||
Nb of lysines | 6 | 12 | 7 | 8 | 9 |
Positions are according to the IMGT unique numbering for C-DOMAIN [1]. For correspondence between the IMGT unique numbering with other numberings, see Correspondence between C numberings.
Sequences are from Homo sapiens IGHG1*01 (J00228), Homo sapiens IGKC*01 (J00241) and Homo sapiens IGLC1*02 (X51755).
In addition to the lysines are shown:
- the five characteristic amino acids of a C-DOMAIN [2,3]. Four of them are highly conserved and hydrophobic [4] and are common to the V domain: C23 (1st-CYS), W41 (CONSERVED-TRP), 89 (hydrophobic) and C104 (2nd-CYS) [5]. These four amino acids contribute to the two major features shared by the V and C domains: the disulfide bridge (between the two cysteines 23 and 104) and the internal hydrophobic core of the domain (with the side chains of tryptophan W41 and amino acid 89) [2,3]. The fifth position, 118 is diverse in the C-DOMAIN and is characterized as being an FG loop anchor (whereas it is conserved in the V-DOMAIN and represented by J-PHE 118 or J-TRP 118).
- the CH2 N84.4 site of N-glycosylation (IMGT Lexique Glycosylation) at the top of the DE turn. The asparagine N84.4 is part of a N-glycosylation motif NXS/T (NST in Homo sapiens IGHG1).
[1] | Lefranc, M.-P., Pommié, C., Kaas, Q., Duprat, E., Bosc, N., Guiraudou, D., Jean, C., Ruiz, M., Da Piedade, I., Rouard, M., Foulquier, E., Thouvenin, V. and Lefranc, G. IMGT unique numbering for immunoglobulin and T cell receptor constant domains and Ig superfamily C-like domains. Dev. Comp. Immunol., 29, 185-203 (2005).PMID: 15572068 with permission from Elsevier. |
[2] | Lefranc, M-P. Immunoglobulin (IG) and T cell receptor genes (TR): IMGT® and the birth and rise of immunoinformatics. Front Immunol. 2014 Feb 05;5:22. doi: 10.3389/fimmu.2014.00022. Open access. PMID: 24600447. |
[3] | Lefranc, M-P. Immunoglobulins: 25 years of Immunoinformatics and IMGT-ONTOLOGY. Biomolecules. 2014, 4(4), 1102-1139; doi:10.3390/biom4041102. Open access. PMID: 25521638. |
[4] | Pommié, C., Levadoux, S., Sabatier, R., Lefranc, G. and Lefranc, M.-P. IMGT standardized criteria for statistical analysis of immunoglobulin V-REGION amino acid properties J. Mol. Recognit., 17, 17-32 (2004). PMID: 14872534 . |
[5] | Lefranc, M.-P., Pommié, C., Ruiz, M., Giudicelli, V., Foulquier, E., Truong, L., Thouvenin-Contet, V. and Lefranc, G. IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains. Dev. Comp. Immunol., 27, 55-77 (2003). PMID: 12477501 with permission from Elsevier. |
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