Conformation of the hypervariable region L3 without the key proline residue.
The refined structure of the Fab fragment of the monoclonal antibody CRIS-I (IgG2a kappa) against the leukocyte differentiation antigen CD5, determined at 1.9 A resolution with an agreement R-factor of 18.3%, reveals a variant of the canonical conformations proposed for the light chain complementarity determining region L3 (CDR-L3). This is the first Fab structure available with a kappa light chain in which the CDR-L3 lacks the key proline residue in either position 94 or 95. The conformation found could be significant for about 10% of the murine IgG molecules with kappa light chains without proline in their CDR-L3 sequences.
Guarné
A
A
Department d'Enginyeria Química, ETSEIB, UPC, Barcelona, Spain.
Bravo
J
J
Calvo
J
J
Lozano
F
F
Vives
J
J
Fita
I
I
D000818:Animals; D003460:Crystallization; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry*; D007135:Immunoglobulin Variable Region; D051379:Mice; D011487:Protein Conformation
D007140:Immunoglobulin Fab Fragments; D007135:Immunoglobulin Variable Region