ETEXT CAMPBELL BIOLOGY IN FOCUS INSTANT
3rd Edition
ISBN: 9780135964422
Author: Urry
Publisher: PEARSON
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Chapter 35.2, Problem 1CC
Summary Introduction
To draw:
A sketch of B cell antigen receptor and to label the V and C regions, antigen binding sites, disulfide bridges and transmembrane region located relative to these regions.
Introduction:
A B-cell antigen receptor is a protein which is a Y-shaped structure. It consists of four poly-peptide chains, the two-heavy chains and two-light chains. The chains are linked by disulphide bridges.
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DRAW IT Sketch a B cell antigen receptor. Label the Vand C regions of the light and heavy chains. Label theantigen-binding sites, disulfide bridges, and transmembrane region. Where are these features located relativeto the V and C regions?
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Consider a pencil-shaped protein with two epitopes, Y (the “eraser” end) and Z (the “point” end). They are recognized by antibodies A1 and A2, respectively. Draw and label a picture showing the antibodies linking proteins into a complex that could trigger endocytosis by a macrophage.
Chapter 35 Solutions
ETEXT CAMPBELL BIOLOGY IN FOCUS INSTANT
Ch. 35.1 - Pus is both a sign of infection and an indicator...Ch. 35.1 - MAKE CONNECTIONS How do the molecules that...Ch. 35.1 - Prob. 3CCCh. 35.2 - Prob. 1CCCh. 35.2 - Explain how memory cells strengthen the immune...Ch. 35.2 - WHAT IF? If both copies of a light-chain gene and...Ch. 35.3 - Prob. 1CCCh. 35.3 - Prob. 2CCCh. 35.3 - Prob. 3CCCh. 35 - Prob. 1TYU
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- Write T if the statement is correct; write F if the statement is not correct. P and E selectins are expressed by endothelial cells. " " TCRs consist of heavy and light chains. " " A disulfide bond can be found on TCRs. " " The antigen binding site in TCRs is contributed by the variable region of the H chain and the variable region of the light chain. " " CD4, but not CD8, interacts with Lck. " "arrow_forwardFor the diagram below, all of the following statements are true EXCEPT: Antigen- binding site V C Heavy chain V Light chain S.S. Fc (stem) region c C Hinge region None of the other four answers (All are true statements) Antibodies (Immunoglobulins) are composed of four protein molecules, two identical "light" chains and two identical "heavy" chains Antigens bind to the "stem", composed of the constant regions of the two "heavy" chains The variable (V) regions form the antigen binding sites The constant (C) regions determine class of antibodyarrow_forwardHow are antibodies unique? Please discuss the structure of an antibody. What are the V and C regions? Discuss how the few hundred genes involved are capable of making endless amounts of antibodies. Besides medical treatment what is another way antibodies can be used?arrow_forward
- Answer c onlyarrow_forwardThe ends of each heavy chain and light chain in an immunoglobulin make up the antigen-binding sites. The end of one of these chains is shown here. Biochemists tend to classify protein structures into four groups: mostly alpha, mostly beta, mixed alpha and beta, or neither alpha nor beta. Based on the model shown here, how would you classify this part of the immunoglobulin protein? The loopy polypeptide segments at the very top of the structure shown are the segments that actually contact the antigen. Would you expect these binding segments to be rigid or flexible?arrow_forwardWhat physiological effect would you predict from a mutation that replacedwith serine the cysteine in the constant part of the immunoglobulin lightchain that is involved in disulfide-bond formation with the heavy chain?(as shown)arrow_forward
- B cells express a complement receptor that binds to C3b cleavage products, such as iC3b and C3dg. When a B cell with an antigen receptor that specifically recognizes that pathogen also has its complement receptor stimulated because the pathogen is opsonized with these C3 fragments, B cell activation is greatly enhanced. Due to this mechanism, B cells can be activated by much lower concentrations of antigen (in this case, the pathogen) than if the antigen is devoid of complement components. This mechanism functions to: Ensure that pathogens are readily detected by the adaptive immune system before they replicate to high levels in the host Prevent B cells from being activated in response to antigens that are not pathogens Allow B cells to phagocytose the pathogen and help destroy it Induce increased rounds of B cell replication to make more pathogen-specific B cells Allow the B cell to block pathogen replication by interfering with multiple pathogen surface functionsarrow_forwardClass II MHC proteins display what kind of antigens? What class of T cell recognizes antigens bound to class II MHC? What types of cells display these proteins?arrow_forwardDraw the structure of an antibody molecule(a typical IgG)and show how this structure enables it to bind to a specific antigen. Include the following terms in your diagranm: heavy chain (H chain), light chain (L chain), variable region, constant region, Fab, Fc, hinge and disulfide bonds.arrow_forward
- Construct a typical antibody (immunoglobulin) molecule. Label the variable and constant regions, and the light and heavy chains. Indicate which region determines the antibody’s isotype (class). Indicate which region determines its antigenic specificity.arrow_forwardCreate a concept map that describes antibodies using the following terms: Antibodies Agglutination Antibody-dependent cell-mediated cytotoxicity (ADDC) Antigens Antigen-stimulated B cells Complement activation IgA IgD IgE IgG IgM Inflammation Neutralization Phagocytosis Plasma cells Secreted immunoglobulinsarrow_forwardDescribe in chronological order the steps involved in the recruitment of neutrophils to infected tissue sites during an innate immune response. Use the following terms in your description: rolling adhesion, tight binding, extravasation, migration, inflammatory mediators, integrins, adhesion molecules, chemokines, selectins, sialyl-Lewisx, and basement membrane proteases.arrow_forward
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