Table 2.
Characteristics of the human LCs used in the study
| LC | Kidney Disease | Isotype | V (L) Domain | Mutations of Interesta | Crystal Formationb | pI (V Domain) | Charge (pH 7/pH 5) | Aggregation Score (V Domain)c | Reference |
|---|---|---|---|---|---|---|---|---|---|
| CH | RFS | κ | Vκ1–39 | A30; I94 | Yes | 8.45 | 1.9/3.2 | 486.69 | 1,6 |
| DU | RFS | κ | Vκ1–5 | V31 | Yes | 5.17 | −1.1/0.4 | 897.65 | — |
| CHm | — | κ | Vκ1–39 | A30→S | No | 8.45 | 1.9/3.2 | 229.12 | 6 |
| DE | AL amyloidosis | κ | Vκ1–33 | F52 | No | 5.36 | −1.1/1.0 | 332.77 | — |
| RO | Cast nephropathy | κ | Vκ2–28 | A51;Y52 | No | 7.09 | 0.1/3.0 | 595.71 | — |
V(L), variable domain; pl, isoelectric point; DU, RFS-kLC; —, not causing kidney disease; AL, amyloid light chain; CDR, complementary determing region; TANGO, algorithm used to predict the aggregating regions in the V(L) domain.
a
Polar to hydrophobic residue substitution in solvent-exposed loops (CDR).
b
Crystal formation was documented by electron microscopy study of the kidney biopsy.
c
Aggregation score obtained using the TANGO algorithm.