binding site Antigen- binding site VH Hlnge reglon S-S Light chaln CHO CH CHO CH 1 FIGURE 7.3 Schematic models of an IgG antibody molecule and an Fab fragment. The IgG is made from two identical heavy chains (dark blue) and two identical light chains (light blue), all held together by disulfide bonds. Each chain contains both constant domains (C) and variable domains (V). Constant domains are the same in all antibody molecules of a given class (see Table 7.1), whereas variable domains confer specificity to a given antigenic determinant. Cleavage by certain proteolytic enzymes such as papain at the hinge regions allows production of two identical monovalent Fab fragments and one F, fragment (see Figure 7.4). The carbohydrate (CHO; red) attached to the heavy chains helps determine the destinations of antibodies in the tissues and in stimulating secondary responses such as phagocytosis. The crystal structure of an immunoglobulin molecule is shown in Figure 7.4. Heavy chaln Enzymatlc dleavage Fab fragments VH VL S-S ss CHO CH CH CHO Fe fragment Antigen-

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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What physiological effect would you predict from a mutation that replaced
with serine the cysteine in the constant part of the immunoglobulin light
chain that is involved in disulfide-bond formation with the heavy chain?
(as shown)

binding site
Antigen-
binding site
VH
Hlnge
reglon
S-S
Light chaln
CHO
CH
CHO
CH
1 FIGURE 7.3 Schematic models of an IgG antibody molecule and an Fab fragment. The
IgG is made from two identical heavy chains (dark blue) and two identical light chains (light
blue), all held together by disulfide bonds. Each chain contains both constant domains
(C) and variable domains (V). Constant domains are the same in all antibody molecules of a
given class (see Table 7.1), whereas variable domains confer specificity to a given antigenic
determinant. Cleavage by certain proteolytic enzymes such as papain at the hinge regions
allows production of two identical monovalent Fab fragments and one F, fragment (see
Figure 7.4). The carbohydrate (CHO; red) attached to the heavy chains helps determine the
destinations of antibodies in the tissues and in stimulating secondary responses such as
phagocytosis. The crystal structure of an immunoglobulin molecule is shown in Figure 7.4.
Heavy chaln
Enzymatlc
dleavage
Fab fragments
VH
VL
S-S
ss
CHO
CH CH
CHO
Fe fragment
Antigen-
Transcribed Image Text:binding site Antigen- binding site VH Hlnge reglon S-S Light chaln CHO CH CHO CH 1 FIGURE 7.3 Schematic models of an IgG antibody molecule and an Fab fragment. The IgG is made from two identical heavy chains (dark blue) and two identical light chains (light blue), all held together by disulfide bonds. Each chain contains both constant domains (C) and variable domains (V). Constant domains are the same in all antibody molecules of a given class (see Table 7.1), whereas variable domains confer specificity to a given antigenic determinant. Cleavage by certain proteolytic enzymes such as papain at the hinge regions allows production of two identical monovalent Fab fragments and one F, fragment (see Figure 7.4). The carbohydrate (CHO; red) attached to the heavy chains helps determine the destinations of antibodies in the tissues and in stimulating secondary responses such as phagocytosis. The crystal structure of an immunoglobulin molecule is shown in Figure 7.4. Heavy chaln Enzymatlc dleavage Fab fragments VH VL S-S ss CHO CH CH CHO Fe fragment Antigen-
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