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Protein Science, Vol 5, Issue 1 167-169, Copyright © 1996 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Conformation of the hypervariable region L3 without the key proline residue

A. GUARNE, J. BRAVO, J. CALVO, F. LOZANO, J. VIVES and I. FITA
Departament d'Enginyeria Quimica, ETSEIB, UPC, Av. Diagonal, 647. 08028 Barcelona, Spain

The refined structure of the Fab fragment of the monoclonal antibody CRIS-1 (IgG2ak) 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 k 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 k light chains without proline in their CDR-L3 sequences.
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