The structure of the hinge region in Fab-Fc recombinant immunoglobulins and its relation to the effector activity of these molecules.
The arrangement of peptides which form the hinge region in Fab-Fc recombinant immunoglobulins, restored artificially from Fab and Fc fragments was approached by computation. The architecture of this region in the symmetric (Fab')2-Fc derivatives and in the asymmetric (Fab')1-Fc differs to a considerable extent. In (Fab')2-Fc species but not in (Fab')1-Fc the preferable arrangement appeared to be stabilized predominantly by the mutual interaction of symmetric hinge peptides. It was concluded that the resulted by this interaction rotational restrictions may eventually induce the structural transformations in the molecule, influencing the effector activity of Fc.
Roterman
I
I
Department of Medical Informatics, Medical Academy, Cracow.
Konieczny
L
L
Bobrzecka
K
K
Rybarska
J
J
Ochalska
B
B
D000595:Amino Acid Sequence; D000818:Animals; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007133:Immunoglobulin Joining Region; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010455:Peptides; D011487:Protein Conformation; D011817:Rabbits; D011994:Recombinant Proteins; D013816:Thermodynamics
D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007133:Immunoglobulin Joining Region; D010455:Peptides; D011994:Recombinant Proteins