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Carbohydrates can play important roles by modulating interactions between proteins. For example, Figure 7-27 (7th ed) shows how heparin (repeating unit of glycosaminoglycan, see Figure 7-22) binding can modulate the interaction between thrombin and anti- thrombin. What role do the sulfates of heparin play in stabilizing this complex, and what is the consequence of that stabilization? Select one: O a. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. b. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex keeps the protease (thrombin) from initiating the coagulation cascade. O c. The sulfates bind to pockets on both proteins lined with arginine and lysine residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. O d. The sulfates bind to pockets on both proteins lined with glycine and proline residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade.

Carbohydrates can play important roles by modulating interactions between proteins. For example, Figure 7-27 (7th ed) shows how heparin (repeating unit of glycosaminoglycan, see Figure 7-22) binding can modulate the interaction between thrombin and anti- thrombin. What role do the sulfates of heparin play in stabilizing this complex, and what is the consequence of that stabilization? Select one: O a. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. b. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex keeps the protease (thrombin) from initiating the coagulation cascade. O c. The sulfates bind to pockets on both proteins lined with arginine and lysine residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. O d. The sulfates bind to pockets on both proteins lined with glycine and proline residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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### Figure Explanation #### (a) Syndecan This diagram illustrates the structure of a syndecan, a type of transmembrane proteoglycan. - **Heparan Sulfate Chains**: These are shown extending from the core protein outside the cell membrane. They are depicted as green wavy lines. - **Chondroitin Sulfate Chains**: Illustrated as orange wavy lines, also extending from the core protein. - **Transmembrane Domain**: The core protein, depicted by the pink structure, spans the cell membrane, with the outer section being in the extracellular environment, labeled "Outside," and the inner section labeled "Inside." - **Functional Groups**: The protein features functional groups like \(^+\text{NH}_3\) and \(^-\text{OOC}\), indicating charged regions that could participate in cellular interactions. #### (b) Heparan Sulfate The diagram provides a detailed view of the heparan sulfate chain structure. - **NA and S Domains**: The chain is divided into segments labeled as NA (N-acetylated) and S (sulfated) domains. - **Sugar Components**: The key shows symbols for different sugar residues: - **GlcNAc**: N-acetylglucosamine (hexagon with a red outline) - **GlcA**: Glucuronic acid (hexagon with a purple fill) - **GlcNS**: N-sulfoglucosamine (hexagon with a green fill) - **IdoA**: Iduronic acid (hexagon with a yellow fill) - **Sulfation Marks**: - **2-O-sulfate**: Red downward arrow - **6-O-sulfate**: Red upward arrow This detailed molecular structure demonstrates the complexity and diversity in the binding potential of heparan sulfate chains due to various sulfation patterns.
Transcribed Image Text:### Figure Explanation #### (a) Syndecan This diagram illustrates the structure of a syndecan, a type of transmembrane proteoglycan. - **Heparan Sulfate Chains**: These are shown extending from the core protein outside the cell membrane. They are depicted as green wavy lines. - **Chondroitin Sulfate Chains**: Illustrated as orange wavy lines, also extending from the core protein. - **Transmembrane Domain**: The core protein, depicted by the pink structure, spans the cell membrane, with the outer section being in the extracellular environment, labeled "Outside," and the inner section labeled "Inside." - **Functional Groups**: The protein features functional groups like \(^+\text{NH}_3\) and \(^-\text{OOC}\), indicating charged regions that could participate in cellular interactions. #### (b) Heparan Sulfate The diagram provides a detailed view of the heparan sulfate chain structure. - **NA and S Domains**: The chain is divided into segments labeled as NA (N-acetylated) and S (sulfated) domains. - **Sugar Components**: The key shows symbols for different sugar residues: - **GlcNAc**: N-acetylglucosamine (hexagon with a red outline) - **GlcA**: Glucuronic acid (hexagon with a purple fill) - **GlcNS**: N-sulfoglucosamine (hexagon with a green fill) - **IdoA**: Iduronic acid (hexagon with a yellow fill) - **Sulfation Marks**: - **2-O-sulfate**: Red downward arrow - **6-O-sulfate**: Red upward arrow This detailed molecular structure demonstrates the complexity and diversity in the binding potential of heparan sulfate chains due to various sulfation patterns.
Carbohydrates can play important roles by modulating interactions between proteins. For example, Figure 7-27 (7th ed) shows how heparin (repeating unit of glycosaminoglycan, see Figure 7-22) binding can modulate the interaction between thrombin and anti-thrombin. What role do the sulfates of heparin play in stabilizing this complex, and what is the consequence of that stabilization? Select one: - a. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. - b. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex keeps the protease (thrombin) from initiating the coagulation cascade. - c. The sulfates bind to pockets on both proteins lined with arginine and lysine residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. - d. The sulfates bind to pockets on both proteins lined with glycine and proline residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. - e. The sulfates bind to pockets on both proteins lined with arginine and lysine residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex keeps the protease (thrombin) from initiating the coagulation cascade.
Transcribed Image Text:Carbohydrates can play important roles by modulating interactions between proteins. For example, Figure 7-27 (7th ed) shows how heparin (repeating unit of glycosaminoglycan, see Figure 7-22) binding can modulate the interaction between thrombin and anti-thrombin. What role do the sulfates of heparin play in stabilizing this complex, and what is the consequence of that stabilization? Select one: - a. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. - b. The sulfates bind to pockets on both proteins lined with glutamate and aspartate residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex keeps the protease (thrombin) from initiating the coagulation cascade. - c. The sulfates bind to pockets on both proteins lined with arginine and lysine residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. - d. The sulfates bind to pockets on both proteins lined with glycine and proline residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex activates the protease (thrombin), initiating the coagulation cascade. - e. The sulfates bind to pockets on both proteins lined with arginine and lysine residues. The binding of heparin and the stabilization of the thrombin-anti-thrombin complex keeps the protease (thrombin) from initiating the coagulation cascade.
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