title: Conformations of immunoglobulin hypervariable regions.
abstract: On the basis of comparative studies of known antibody structures and sequences it has been argued that there is a small repertoire of main-chain conformations for at least five of the six hypervariable regions of antibodies, and that the particular conformation adopted is determined by a few key conserved residues. These hypotheses are now supported by reasonably successful predictions of the structures of most hypervariable regions of various antibodies, as revealed by comparison with their subsequently determined structures.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: C
authors.initials: C
authors.lastname: Chothia
authors.forename: A M
authors.initials: AM
authors.lastname: Lesk
authors.forename: A
authors.initials: A
authors.lastname: Tramontano
authors.forename: M
authors.initials: M
authors.lastname: Levitt
authors.forename: S J
authors.initials: SJ
authors.lastname: Smith-Gill
authors.forename: G
authors.initials: G
authors.lastname: Air
authors.forename: S
authors.initials: S
authors.lastname: Sheriff
authors.forename: E A
authors.initials: EA
authors.lastname: Padlan
authors.forename: D
authors.initials: D
authors.lastname: Davies
authors.forename: W R
authors.initials: WR
authors.lastname: Tulip
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D007135:Immunoglobulin Variable Region; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D007135:Immunoglobulin Variable Region