title: Structural classification of CDR-H3 in antibodies.
abstract: 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.
authors.affiliation: Department of Bioinformatics, Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Shirai
authors.forename: A
authors.initials: A
authors.lastname: Kidera
authors.forename: H
authors.initials: H
authors.lastname: Nakamura
mesh_terms: 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
chemical_list: D000906:Antibodies; D007135:Immunoglobulin Variable Region