Chapter 11: Problem 40
REFLECT AND APPLY Give examples of structural motifs found in transcription factors that interact with other proteins instead of DNA.
Short Answer
Expert verified
Examples of structural motifs in transcription factors that interact with other proteins include the SH2 domain, SH3 domain, and WD40 repeat motif.
Step by step solution
01
- Understand Structural Motifs
Structural motifs in proteins are specific arrangements of secondary structures (like alpha-helices and beta-strands) that are common across different proteins and are associated with specific biological functions. Some motifs facilitate the interaction of transcription factors with other proteins.
02
- Identify Common Interaction Motifs
Research and list common structural motifs found in transcription factors that interact with other proteins. Some well-known examples include the SH2 domain, SH3 domain, and WD40 repeat motif.
03
- Explain the SH2 Domain
The SH2 (Src Homology 2) domain is a protein domain that allows protein-protein interactions through binding to phosphorylated tyrosines found in other proteins.
04
- Explain the SH3 Domain
The SH3 (Src Homology 3) domain is a small protein domain that binds to proline-rich motifs in other proteins, mediating protein-protein interactions.
05
- Explain the WD40 Repeat Motif
The WD40 repeat motif consists of several repeating units that form a beta-propeller structure, facilitating interactions with various proteins through its stable and versatile surface.
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Key Concepts
These are the key concepts you need to understand to accurately answer the question.
SH2 domain
The SH2 (Src Homology 2) domain is a commonly found motif in proteins that facilitates protein-protein interactions. This domain specifically binds to phosphorylated tyrosines on other proteins.
Phosphorylation is a process where a phosphate group is added to a protein, which can alter its function and activity.
The ability of SH2 domains to recognize and bind phosphorylated tyrosines is crucial for various cellular processes including signal transduction, where cells respond to signals from their external environment. This makes SH2 domains an essential part of many signaling pathways.
Phosphorylation is a process where a phosphate group is added to a protein, which can alter its function and activity.
The ability of SH2 domains to recognize and bind phosphorylated tyrosines is crucial for various cellular processes including signal transduction, where cells respond to signals from their external environment. This makes SH2 domains an essential part of many signaling pathways.
- Binding Specificity: SH2 domains are highly specific, recognizing the phosphorylated tyrosine within a particular sequence context.
- Function in Transcription Factors: Through these interactions, transcription factors containing SH2 domains can be recruited to specific locations in the cell, where they will affect the transcription of genes.
SH3 domain
The SH3 (Src Homology 3) domain is another structural motif that is critical for protein-protein interactions, especially in the context of cellular signaling. Unlike the SH2 domain which binds to phosphorylated tyrosines, the SH3 domain binds to proline-rich sequences in target proteins.
Proline-rich sequences refer to regions within proteins that have a high number of proline amino acids. This specific binding ensures that proteins with SH3 domains can interact selectively with other proteins that contain these motifs.
Proline-rich sequences refer to regions within proteins that have a high number of proline amino acids. This specific binding ensures that proteins with SH3 domains can interact selectively with other proteins that contain these motifs.
- Proline-Rich Motifs: The SH3 domain interacts with short stretches rich in proline residues, playing an essential role in assembling protein complexes.
- Biological Processes: Critical in many cellular processes like cytoskeleton reorganization, which helps cells maintain their shape, and in signal transduction pathways.
- Function in Transcription Factors: In transcription factors, SH3 domains help in recruiting and anchoring the proteins to precise locations, ensuring that genes are expressed accurately when required.
WD40 repeat motif
The WD40 repeat motif is a multi-repeat protein domain known for its role in facilitating protein-protein interactions. Characterized by a series of repeating units, this motif typically forms a circular beta-propeller structure, which provides a stable platform for various interactions.
The beta-propeller structure makes the WD40 motif highly versatile, allowing it to interact with multiple proteins simultaneously.
The beta-propeller structure makes the WD40 motif highly versatile, allowing it to interact with multiple proteins simultaneously.
- Structure: Composed of 4-8 repeating units, each forming a strand, which together create the propeller-like shape.
- Functionality: Provides a rigid and versatile protein surface for binding a wide variety of proteins, including those involved in gene regulation, signal transduction, and vesicular trafficking.
- Importance in Transcription Factors: WD40 motifs enable transcription factors to form complexes with other proteins, facilitating the regulation of gene expression by bringing together various components required for the transcription process.