Figure 3-42. An antibody molecule.

Figure 3-42An antibody molecule

(A) A typical antibody molecule is Y-shaped and has two identical binding sites for its antigen, one on each arm of the Y. The protein is composed of four polypeptide chains (two identical heavy chains and two identical and smaller light chains) held together by disulfide bonds. Each chain is made up of several different immunoglobulin domains, here shaded either blue or gray. The antigen-binding site is formed where a heavy-chain variable domain (VH) and a light-chain variable domain (VL) come close together. These are the domains that differ most in their sequence and structure in different antibodies. (B) This ribbon model of a light chain shows the parts of the VL domain most closely involved in binding to the antigen in red. They contribute half of the fingerlike loops that fold around each of the antigen molecules in (A).

From: Protein Function

Cover of Molecular Biology of the Cell
Molecular Biology of the Cell. 4th edition.
Alberts B, Johnson A, Lewis J, et al.
New York: Garland Science; 2002.
Copyright © 2002, Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, and Peter Walter; Copyright © 1983, 1989, 1994, Bruce Alberts, Dennis Bray, Julian Lewis, Martin Raff, Keith Roberts, and James D. Watson .

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