See figure 12.16b regarding the process by which cyclin regulates the Cdk. Suppose that the cyclin binding site in the Cdk contains these FOUR amino acids in this order from top to bottom: serine, lysine, aspartic acid acid and lysine and the Cdk binding site in the cyclin contains these FOUR amino acids in this order from top to bottom: aspartic acid, aspartic acid, lysine and serine. Use the schematics below to show the R groups and how they might interact to create the cyclin-cdk complex. Label both binding sites, show all charges that will be used to create any bonds, and label all bonds formed and add the ATP active site. PA Explain what a kinase does and how the cyclin controls the activity of the Cdk.

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### Figure 12.16b: Cyclin Regulation of Cdk

This figure illustrates the molecular interaction between cyclin and cyclin-dependent kinase (Cdk), essential for cell cycle regulation.

#### Details:

- **Cyclin Binding Site in Cdk:** Contains four amino acids in this order from top to bottom:
  - Serine
  - Lysine
  - Aspartic Acid
  - Lysine

- **Cdk Binding Site in Cyclin:** Contains four amino acids in this order from top to bottom:
  - Aspartic Acid
  - Aspartic Acid
  - Lysine
  - Serine

The schematic shows two irregular shapes representing the binding sites of Cdk and cyclin. The protrusions and indentations suggest possible points of interaction where bonds may form.

#### Instructions:

- Use the amino acid sequences to determine the R-group interactions.
- Label the binding sites, noting the charges that facilitate bonding.
- Identify all bonds formed and mark the ATP active site within the complex.

#### Additional Explanation:

- **Function of a Kinase:** 
  - A kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy molecules (like ATP) to specific substrates. This process is known as phosphorylation and is crucial for regulating cellular activities.

- **Role of Cyclin in Cdk Activity:**
  - Cyclins are proteins that control the progression of cells through the cell cycle by activating Cdks. When cyclin binds to Cdk, it triggers a conformational change, enabling Cdk's kinase activity. This activation is essential for cell cycle transitions, such as moving from the G1 phase to the S phase.

This detailed understanding of cyclin-Cdk interactions is fundamental for comprehending cell cycle regulation and its implications in cellular proliferation and cancer research.
Transcribed Image Text:### Figure 12.16b: Cyclin Regulation of Cdk This figure illustrates the molecular interaction between cyclin and cyclin-dependent kinase (Cdk), essential for cell cycle regulation. #### Details: - **Cyclin Binding Site in Cdk:** Contains four amino acids in this order from top to bottom: - Serine - Lysine - Aspartic Acid - Lysine - **Cdk Binding Site in Cyclin:** Contains four amino acids in this order from top to bottom: - Aspartic Acid - Aspartic Acid - Lysine - Serine The schematic shows two irregular shapes representing the binding sites of Cdk and cyclin. The protrusions and indentations suggest possible points of interaction where bonds may form. #### Instructions: - Use the amino acid sequences to determine the R-group interactions. - Label the binding sites, noting the charges that facilitate bonding. - Identify all bonds formed and mark the ATP active site within the complex. #### Additional Explanation: - **Function of a Kinase:** - A kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy molecules (like ATP) to specific substrates. This process is known as phosphorylation and is crucial for regulating cellular activities. - **Role of Cyclin in Cdk Activity:** - Cyclins are proteins that control the progression of cells through the cell cycle by activating Cdks. When cyclin binds to Cdk, it triggers a conformational change, enabling Cdk's kinase activity. This activation is essential for cell cycle transitions, such as moving from the G1 phase to the S phase. This detailed understanding of cyclin-Cdk interactions is fundamental for comprehending cell cycle regulation and its implications in cellular proliferation and cancer research.
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