Conformations of immunoglobulin hypervariable regions

@article{Chothia1989ConformationsOI,
  title={Conformations of immunoglobulin hypervariable regions},
  author={C. Chothia and A. Lesk and A. Tramontano and M. Levitt and S. Smith‐Gill and G. Air and S. Sheriff and E. Padlan and D. Davies and W. R. Tulip and P. Colman and S. Spinelli and P. Alzari and R. Poljak},
  journal={Nature},
  year={1989},
  volume={342},
  pages={877-883}
}
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… Expand
Homology modeling of antibody combining sites
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Using database screening techniques, the relationship between antigen‐binding loops in immunoglobulins, and regions of similar conformation in other protein families are examined and model building is assessed by data base screening, compared with that based on canonical structures. Expand
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Antibody structure, prediction and redesign.
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Conformations of the third hypervariable region in the VH domain of immunoglobulins.
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The general conclusion of this work is that the conformation of H3 shows some regularities, from which rules relating sequence to conformation can be stated, but to a less complete degree than for the other five antigen-binding loops. Expand
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Several remarkable rules are derived, which could partly govern the CDR‐H3 conformation dependence on the sequence, and are expected to be applicable to structural modeling and design of antibodies. Expand
Length distribution of CDRH3 in antibodies
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This enormous length variation of CDRH3, together with amino acid substitutions in their sequences, can provide a very large number of antibody specificities and can influence the shape of antibody combining sites. Expand
Structural determinants in the sequences of immunoglobulin variable domain.
TLDR
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