Dynamic aspects of antibody structure.
نویسندگان
چکیده
The flexible nature of immunoglobulins is clearly demonstrated in electron micrographs of antibody complexes, and serves as the structural basis for the interpretation of time-resolved fluorescence depolarization studies. The extent of the flexibility seen with the electron microscope (EM) will be the initial topic of this review. We will compare rabbit polyclonal and mouse monoclonal antibodies, demonstrating by electron microscopy some interesting differences in flexibilities; the contrast provides new information. A direct approach to immunoglobulin dynamics through time-resolved fluorescence depolarization is discussed in the second part, and a simple theoretical interpretation is elaborated in some detail. Anisotropy decay curves for rabbit, human and mouse IgG antibodies are analysed in the light of this simple theory. Immunoglobulin dynamics, as measured by time-resolved fluorescence depolarization, is interpreted in terms of the flexible structures seen in the electron micrographs. The length of the upper hinge polypeptide is the predominant structural feature which determines both the long correlation time of the anisotropy decay curves and the percentage of closed-hinge dimers seen in the electron micrographs. It is suggested that interactions between residues of the hinge and the C-terminal portions of first constant domains are responsible for the restriction in flexibility associated with short hinge length.
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عنوان ژورنال:
- Molecular immunology
دوره 28 12 شماره
صفحات -
تاریخ انتشار 1991