Synthetic peptides VH(27-68) and VH(16-68) of the myeloma immunoglobulin M603 heavy chain and their association with the natural light chain to form an antigen binding site

Biochemistry ◽  
1987 ◽  
Vol 26 (24) ◽  
pp. 7849-7855 ◽  
Author(s):  
Teresa Kubiak ◽  
Donald B. Whitney ◽  
R. B. Merrifield
Keyword(s):  
Binding Site ◽  
Heavy Chain ◽  
Light Chain ◽  
Synthetic Peptides ◽  
Antigen Binding ◽  
Natural Light ◽  
Antigen Binding Site

scholarly journals A shared idiotype among human anti-Ro/SSA autoantibodies.

1989 ◽  
Vol 169 (5) ◽  
pp. 1583-1588 ◽  
Author(s):  
K K Gaither ◽  
J B Harley
Keyword(s):  
Binding Site ◽  
Heart Block ◽  
Congenital Heart ◽  
Congenital Heart Block ◽  
Antigen Binding ◽  
Normal Donor ◽  
Neonatal Lupus ◽  
Antigen Binding Site ◽  
Fine Specificity ◽  
Low Level

Idiotypes and antiidiotypes are thought to be important immune regulators and have provided clues for the origin and pathogenicity of autoantibodies. Many lupus and Sjögren's syndrome patients, as well as most neonatal lupus infants with congenital heart block or dermatitis, have antibodies to the ribonucleoprotein Ro/SSA, which is one of a group of RNA-protein autoantigens commonly found in human lupus sera. To characterize the fine specificity of anti-Ro/SSA antibodies, a rabbit antidiotypic serum was prepared against polyclonal affinity purified anti-Ro/SSA F(ab')2. The resulting antiidiotype, anti-Id-Rol, is specific for the F(ab')2 fraction of the anti-Ro/SSA immunogen and its binding to anti-Ro/SSA is inhibited by purified Ro/SSA. These data indicate that the Id-Rol epitope on anti-Ro/SSA is associated with the antigen binding site of these same antibodies. The Id-Rol idiotype was present by ELISA in 3 of 12 additional anti-Ro/SSA preparations from precipitin-positive donor sera and in anti-Ro/SSA from one normal donor with low level antibody. This is the first shared idiotype to be found in the human autoantibodies binding to this RNA-protein antigen. Idiotypic differences between anti-Ro/SSA autoantibodies have the potential to explain the variation in pathologic associations found in individuals who develop this autoantibody specificity.

THE THREE-DIMENSIONAL STRUCTURE OF THE ANTIGEN BINDING SITE OF McPC 603 PROTEIN

1974 ◽  
pp. 7-14 ◽  
Author(s):  
E.A. Padlan ◽  
D.M. Segal ◽  
G.H. Cohen ◽  
D.R. Davies ◽  
S. Rudikoff ◽  
...  
Keyword(s):  
Binding Site ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Antigen Binding ◽  
Antigen Binding Site ◽  
Three Dimensional Structure

scholarly journals Dynamic plasticity of the lipid antigen-binding site of CD1d is crucially favoured by acidic pH and helper proteins

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Bruno Cuevas-Zuviría ◽  
Marina Mínguez-Toral ◽  
Araceli Díaz-Perales ◽  
María Garrido-Arandia ◽  
Luis F. Pacios
Keyword(s):  
Binding Site ◽  
Antigen Binding ◽  
Acidic Ph ◽  
Antigen Binding Site ◽  
Lipid Antigen ◽  
Dynamic Plasticity

Role of the mobility of antigen binding site in high affinity antibody elucidated by surface plasmon resonance

2016 ◽  
Vol 161 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Natsuki Fukuda ◽  
Yoshiaki Suwa ◽  
Makiyo Uchida ◽  
Yoshihiro Kobashigawa ◽  
Hideshi Yokoyama ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Binding Site ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Antigen Binding ◽  
Antigen Binding Site ◽  
High Affinity

Humanization of a highly stable single-chain antibody by structure-based antigen-binding site grafting

2008 ◽  
Vol 45 (9) ◽  
pp. 2474-2485 ◽  
Author(s):  
Maria Elena Villani ◽  
Veronica Morea ◽  
Valerio Consalvi ◽  
Roberta Chiaraluce ◽  
Angiola Desiderio ◽  
...  
Keyword(s):  
Binding Site ◽  
Antigen Binding ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Antigen Binding Site
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