title: Conformation of the hypervariable region L3 without the key proline residue.
abstract: 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.
authors.affiliation: Department d'Enginyeria Química, ETSEIB, UPC, Barcelona, Spain.
authors.forename: A
authors.initials: A
authors.lastname: Guarné
authors.forename: J
authors.initials: J
authors.lastname: Bravo
authors.forename: J
authors.initials: J
authors.lastname: Calvo
authors.forename: F
authors.initials: F
authors.lastname: Lozano
authors.forename: J
authors.initials: J
authors.lastname: Vives
authors.forename: I
authors.initials: I
authors.lastname: Fita
mesh_terms: D000818:Animals; D003460:Crystallization; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry*; D007135:Immunoglobulin Variable Region; D051379:Mice; D011487:Protein Conformation
chemical_list: D007140:Immunoglobulin Fab Fragments; D007135:Immunoglobulin Variable Region