Structural classification of CDR-H3 in antibodies.
Large varieties in the lengths and the amino acid sequences of the third complementarity determining region of the antibody heavy chain (CDR-H3) have made it difficult to establish a relationship between the sequences and the tertiary structures, in contrast to the other CDRs, which are classified by their canonical structures. A total of 55 CDR-H3 segments from well determined crystal structures were analyzed, and we have derived several remarkable rules, which could partly govern the CDR-H3 conformation dependence on the sequence. Since the rules are physically reasonable, they are expected to be applicable to structural modeling and design of antibodies.
Shirai
H
H
Department of Bioinformatics, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
Kidera
A
A
Nakamura
H
H
D000595:Amino Acid Sequence; D000906:Antibodies / Q000737:chemistry*; D018360:Crystallography, X-Ray; D007135:Immunoglobulin Variable Region / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D000906:Antibodies; D007135:Immunoglobulin Variable Region