| First Author | Ge L | Year | 1995 |
| Journal | J Biol Chem | Volume | 270 |
| Issue | 21 | Pages | 12446-51 |
| PubMed ID | 7759486 | Mgi Jnum | J:25639 |
| Mgi Id | MGI:73353 | Doi | 10.1074/jbc.270.21.12446 |
| Citation | Ge L, et al. (1995) A mouse Ig kappa domain of very unusual framework structure loses function when converted to the consensus. J Biol Chem 270(21):12446-51 |
| abstractText | Antibody gene sequences, particularly those of kappa light chains, are very well conserved in the framework region, and the variability is concentrated in the complementarity-determining regions (CDR). We now found that the murine antibody 93-6 (Djavadi-Ohaniance, L., Friguet, B., and Goldberg, M. (1984) Biochemistry 23, 97-104) whose Fab fragment binds the beta-subunit of Escherichia coli tryptophan synthase with high affinity (Kd of 6.7.10(-9) M) has a highly unusual kappa light chain framework, which is crucial for the function of this antibody. It carries an insertion of 8 amino acids in a conserved framework loop that faces the antigen, and its framework region 2 (FR2) which precedes CDR2 is shortened by one amino acid, normally leucine and part of an absolutely conserved beta-bulge preceding CDR2. Removal of the insertion to restore the consensus sequence reduced the binding affinity of 93-6 by a factor 3, while insertion of the missing leucine into FR2 completely abolished binding. |
