Monoclonal Antibody structure

Rezacova P, et al. Structural basis of HIV-1 and HIV-2 protease inhibition by a monoclonal antibody. Structure 2001 9 887-895. 

Monoclonal antibody structural features, such as carbohydrate side chains, influence tissue uptake and clearance (11). For example, Morell and colleagues (76) demonstrated that removal of sialic acid residue from the carbohydrate side chain of mouse IgGj increased its clearance and shortened its half-life. They also demonstrated increased clearance and liver uptake of asialo-a2-iTiacroglobulin and asialohaptoglobin. 

Electron Paramagnetic Resonance Spectroscopy Studies of Immobilized Monoclonal Antibody Structure and Function... 

Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 36 1581-1597, 1997. 

Figure 17.2 An example of prediction of the conformations of three CDR regions of a monoclonal antibody (top row) compared with the unrefined x-ray structure (bottom row). LI and L2 are CDR regions of the light chain, and HI is from the heavy chain. The amino acid sequences of the loop regions were modeled by comparison with the sequences of loop regions selected from a database of known antibody structures. The three-dimensional structure of two of the loop regions, LI and L2, were in good agreement with the preliminary x-ray structure, whereas HI was not. However, during later refinement of the x-ray structure errors were found in the conformations of HI, and in the refined x-ray structure this loop was found to agree with the predicted conformations. In fact, all six loop conformations were correctly predicted in this case. (From C. Chothia et al.. Science 233 755-758, 1986.)...

Information about the putative folding of the H,K-ATPase catalytic subunit through the membrane has been obtained by the combined use of hydropathy analysis according to the criteria of Kyte and Doolittle [51], identification of sites sensitive to chemical modification [46,48,50,52-55], and localization of epitopes of monoclonal antibodies [56]. The model of the H,K-ATPase catalytic subunit (Fig. 1) which has emerged from these studies shows ten transmembrane segments and contains cytosolic N- and C-termini [53]. This secondary structure of the catalytic subunit is probably a common feature of the catalytic subunits of P-type ATPases, since evidence supporting a ten a-helical model with cytosolic N- and C-termini has also been published recently for both Ca-ATPase of the sarcoplasmic reticulum and Na,K-ATPase [57-59]. 

Figure 13 Structures of haptens used for immunizing and coating antigens in a monoclonal antibody-based immunoassay for diuron. A sensitive assay was developed using coating hapten I that had the handle in a position different from the immunogen hapten. When the oxygen in the urea moiety of hapten I was replaced with a sulfur (hapten 11), increasing the heterology, even greater sensitivity was achieved...

Another difficulty is that a peptide may be able to bind to an existing neutralizing monoclonal antibody by an induced-fit mechanism that is somehow driven by the pre-existing structure of the antibody paratope. However, the same induced-fit process may not take place when the peptide is used as the immunogen and is confronted in the host by a large population of B cell receptors allowing a variety of other interactions. 

In cultures of the more resistant cell line, MDCK, the predominant effect of Tyv-specific monoclonal antibodies is to exclude larvae from the monolayer. This exclusion is associated with the formation of cap-like structures that cover the stoma of the larva. Such caps were first described... 

Page, A.P., Hamilton, A.J. and Maizels, R.M. (1992a) Toxocara canis. monoclonal antibodies to carbohydrate epitopes of secreted (TES) antigens localize to different secretion-related structures in infective larvae. Experimental Parasitobgi 75, 56-71. 

Xu et al. [5] described the effect of (z>)-penicillamine on the binding of several antiacetylcholine receptor monoclonal antibodies to the Torpedo acetylcholine receptor. Penicillamine is covalently incorporated into the acetylcholine receptor through SS exchange at the cysteine residues of the a-subunit, altering the antigenic structure of the receptor. This effect on the structure of the native receptor at the neuromuscular junction may be responsible for the establishment of the autoimmune response to the acetylcholine receptor in (i))-penicillamine-induced myasthenia gravis. Cysteine and penicillamine interact to form penicillamine-cysteine mixed disulfide complexes [6] ... 

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