Antibody structure, prediction and redesign

V. Morea, A. Tramontano, M. Rustici, C. Chothia, Arthur Lesk

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

So far the difficulty to predict the structure of the third hypervariable loop of the heavy chain of antibodies has represented the main limitation in modelling the complete antigen binding site. We carefully analysed all available structures of immunoglobulins searching for rules relating the loop conformation to its amine acid sequence. Here, we analyse the conformation of this loop and show that we life able to predict the conformation of the ten residues proximal to the framework. The conformation of the remaining residues of loops longer than 10 residues ban also be predicted in many cases. This, combined with the previously defined canonical structures for the other five hypervariable loops, is an important step toward the prediction of the complete immunoglobulin antigen-binding site. We exemplify our prediction protocol using three known immunoglobulin structures as test cases.

Original languageEnglish (US)
Pages (from-to)9-16
Number of pages8
JournalBiophysical Chemistry
Volume68
Issue number1-3
DOIs
StatePublished - Oct 1 1997

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Organic Chemistry

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