Evidence for Involvement of a Hydrophobic Patch in Framework Region 1 of Human V4-34-Encoded Igs in Recognition of the Red Blood Cell I Antigen

• Published in: The Journal of immunology (1950) Vol. 169; no. 7; pp. 3777 - 3782
• Main Authors: Potter, Kathleen N, Hobby, Paul, Klijn, Susanne, Stevenson, Freda K, Sutton, Brian J
• Format: Journal Article
• Language: English
• Published: United States Am Assoc Immnol 01.10.2002
• Subjects: Agglutinins - metabolism; Amino Acid Sequence; Amino Acid Substitution - genetics; Amino Acid Substitution - immunology; Antibodies, Monoclonal - genetics; Antibodies, Monoclonal - metabolism; Binding Sites, Antibody - genetics; Cell Line, Transformed; Complementarity Determining Regions - chemistry; Complementarity Determining Regions - metabolism; Cryoglobulins; Glycosphingolipids - immunology; Glycosphingolipids - metabolism; Humans; Hydrophobic and Hydrophilic Interactions; Immunoglobulin Heavy Chains - chemistry; Immunoglobulin Heavy Chains - genetics; Immunoglobulin Heavy Chains - metabolism; Immunoglobulin Idiotypes - biosynthesis; Immunoglobulin Idiotypes - genetics; Immunoglobulin Idiotypes - metabolism; Immunoglobulin Variable Region - chemistry; Immunoglobulin Variable Region - genetics; Immunoglobulin Variable Region - metabolism; Immunoglobulin Variable Region - physiology; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins - biosynthesis; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Serine - genetics; Tryptophan - genetics

The monoclonal IgM cold agglutinins that bind to the I/i carbohydrate Ags on the surface of RBCs all have Ig H chains encoded by the V4-34 gene segment. This mandatory use indicates that distinctive amino acid sequences may be involved in recognition. Critical amino acids exist in framework region 1...