Bos taurus ultralong CDR H3 antibodies.
Cow antibodies are unusual in having an exceptionally long third complementarity determining region of the heavy chain (CDR H3). These CDR H3s have a multitude of cysteines and form a distinct domain characterized by a β-ribbon 'stalk' and disulfide bonded 'knob'. Cows appear to utilize somatic hypermutation of a single VDJ rearrangement to produce an astounding variety of distinct CDR H3 sequences with different disulfide bonding patterns within the knob. Thus, cows may be unique amongst vertebrates in evolving an antibody system with both a different scaffold for binding antigen as well as an unusual diversity creating process.
Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines, La Jolla, CA 92037, United States.
Melissa L
ML
Vadnais
Department of Cell and Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines, La Jolla, CA 92037, United States. Electronic address: vvsmider@scripps.edu.
Vaughn V
VV
Smider
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D022801:Complementarity Determining Regions / Q000737:chemistry* / Q000276:immunology; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry* / Q000276:immunology
D022801:Complementarity Determining Regions; D007143:Immunoglobulin Heavy Chains