By D. Scott Linthicum, Nadir R. Farid
Here is an updated evaluation of vital new equipment and ends up in anti-idiotypes, receptors, and molecular mimicry.It starts off with a dialogue of the theoretical historical past ofthe anti-idiotypic community, it really is function within the legislation of immune reaction, and the actual features of anti-idiotypic antibodies. It then is going directly to discover many exciting purposes in such parts as insulin motion, thyroid mobilephone functionality, the neurosciences, cardiology, virology, pharmacology, and copy.
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Additional info for Anti-Idiotypes, Receptors, and Molecular Mimicry
A search for site-filling ligands in the Mcg Bence-Jones dimer: crystal binding studies of fluorescent compounds. Mol. Immunol. 21:561. 9. R. B. Edmundson. 1985. Pressure-induced conformational changes in a human Bence-Jones protein (Mcg). Biochemistry 24:3453. 10. R. B. Edmundson. 1980. Obligatory hybridization of heterologous immunoglobulin light chains into covalently linked dimers. Biochemistry 19:2827. II. L. Z. E. Hayden, and A. Basten. 1983. A tumour associated antigen specific for human kappa-myeloma cells.
Exp. Med. 162:487. 5. P. A. Carson 1985. Synthetic peptides corresponding to third hypervariable region of human monoclonal IgM rheumatoid factor heavy chains define an immunodominant idiotype. J. Exp. Med. 162:756. 6. F. Deutsch. 1974. L chain. Biochemistry 13:4102. 7. R. L. E. Abola, M. A. D. F. Deutsch. 1974. Binding of 2,4-dinitrophenyl compounds and other small molecules to a crystalline lambda type BenceJones dimer. Biochemistry 13:3816. 8. R. N. Herron 1984. A search for site-filling ligands in the Mcg Bence-Jones dimer: crystal binding studies of fluorescent compounds.
Of the nine residues which form the outer rim of the binding cavity of the dimer, aspartic acid 97 is the only residue contributed exclusively by monomer 2. This residue is not found in a comparable location in monomer I and is not present in the sequences of ViI and Weir, which fail to express the idiotope. The negatively charged side chain of aspartic acid is appropriate for interactions with the positively charged rhodamine ligand. Finally, the positioning of aspartic acid 97 in the third hypervariable loop places its side chain in a region which is very accessible for external interactions.