Expressed Murine and Human CDR-H3 Intervals of Equal Length Exhibit Distinct Repertoires that Differ in their Amino Acid Composition and Predicted Range of Structures

• Published in: Journal of molecular biology 2003-12, Vol.334 (4), p.733-749
• Main Authors: Zemlin, Michael, Klinger, Martin, Link, Jason, Zemlin, Cosima, Bauer, Karl, Engler, Jeffrey A., Schroeder, Harry W., Kirkham, Perry M.
• Format: Article
• Language: English
• Subjects: amino acid composition; Amino Acid Sequence; Animals; antibody engineering; Complementarity Determining Regions - chemistry; Complementarity Determining Regions - genetics; Complementarity Determining Regions - metabolism; Crystallography, X-Ray; Cysteine - metabolism; Humans; immunoglobulin heavy chain complementarity-determining region 3; Immunoglobulin Heavy Chains - chemistry; Immunoglobulin Heavy Chains - genetics; Immunoglobulin Heavy Chains - metabolism; intra-chain disulfide bonds; Mice; Models, Molecular; Molecular Sequence Data; predicted structure; Protein Conformation; Sequence Alignment; Sequence Homology, Amino Acid
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/j.jmb.2003.10.007

Immunoglobulin junctional diversity is concentrated in the third complementarity-determining region of the heavy chain (CDR-H3), which often plays a dominant role in antigen binding. The range of CDR-H3 lengths in mouse is shorter than in human, and thus the murine repertoire could be presumed to be a subset of the human one. To test this presumption, we analyzed 4751 human and 2170 murine unique, functional, published CDR-H3 intervals. Although tyrosine, glycine, and serine were found to predominate in both species, the human sequences contained fewer tyrosine residues, more proline residues, and more hydrophobic residues ( p