Each of the six CDRs of Gloop2 is shown with the modeled structure in. Overall, the results
obtained using the combined algorithm are similar in accuracy to those achieved using the …

Publisher Summary This chapter describes the modeling of the antigen-binding sites of
antibodies. The chapter reviews the various modeling procedures that have been applied to …

To be of any value, a predicted model of an antibody combining site should have an
accuracy approaching that of antibody structures determined by x-ray crystallography (1.6 …

The structure of the most variable antibody hypervariable loop, CDR-H3, has been predicted
from amino acid sequence alone. In contrast to other approaches predictions are made for …

Through a conformation search by a simulation calculation, the relationships between the
amino acid sequences and the conformations of the third complementarity‐determining …

The third complementary determining region of the immunoglobulin heavy chain (CDR H3)
is one of the more difficult structures to model due to genetic reasons. However, the …

Predicting the conformations of loops is a critical aspect of protein comparative (homology)
modeling. Despite considerable advances in developing loop prediction algorithms, refining …

The conformation of five of the six hypervariable loops that form the antigen‐binding site of
antibodies is limited to a small set of structures designated as canonical structures. The …

A computer-based algorithm was used to cluster the loops forming the complementarity
determining region (CDR) 3 of the heavy chain (H3) into canonical classes. Previous …

A model of the BR96 antibody variable regions is compared to two X‐ray structures of a
BR96–carbohydrate complex, independently determined after the model was built and …