Related Experiment Video
Updated: Jun 26, 2026
10:21
Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Structure and function of the phosphothreonine-specific FHA domain
Anjali Mahajan1, Chunhua Yuan, Hyun Lee
1Biophysics Program, Ohio State University, Columbus, OH 43210, USA.
Science Signaling
|December 26, 2008
Summary
The forkhead-associated (FHA) domain uniquely binds phosphothreonine (pThr) residues. FHA domains show diverse binding patterns and functions, particularly in DNA damage response.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- The forkhead-associated (FHA) domain is a unique phosphoprotein-binding domain.
- It specifically recognizes phosphothreonine (pThr) residues, differentiating them from phosphoserine (pSer).
Purpose of the Study:
- To review the diverse biological functions of FHA domain-containing proteins.
- To explore the structural basis for FHA domain binding specificities and modes.
Main Methods:
- Literature review of studies on FHA domain structure and function.
- Analysis of FHA domain interactions with various protein targets.
Main Results:
- FHA domains exhibit strict pThr specificity but recognize diverse surrounding residue patterns.
- Examples include Ki67 FHA domain binding to extended surfaces and Dun1 FHA domain recognizing doubly phosphorylated Thr-Gln clusters.
- FHA domains are prevalent in DNA damage response proteins.
Conclusions:
- FHA domains display remarkable versatility in binding specificities and modes.
- Their diverse functions underscore their importance in cellular processes, especially DNA repair.
Related Concept Videos
02:26Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
01:18ATP Synthase: Structure
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...