WD40 repeat proteins commonly form seven-bladed beta-propellers that function as versatile platforms for protein interactions, signaling, transcription, protein degradation, and cellular regulation.
Beta-propeller proteins can be classified by blade number, sequence repeats, structural features, and biological function. Explore four-, five-, six-, seven-, and eight-bladed beta-propellers, WD40 and Kelch proteins, and important examples.
The beta-propeller is a distinctive protein fold formed by multiple beta-sheet blades arranged around a central axis. Learn how its blades, loops, hydrogen bonds, and central region determine its structure and function.
A beta-propeller is a versatile protein fold composed of multiple beta-sheet blades arranged around a central axis. Learn about its structure, types, functions, evolution, and role in enzymes and protein–protein interactions.
PQQ repeats are protein sequence motifs associated with beta-propeller structures in several enzyme families. Learn how these repeats help organize protein architecture and support the function of PQQ-dependent enzymes, including methanol dehydrogenase.
Asp-box repeats are short sequence and structural motifs found in several protein families. Learn how their beta-hairpin structure helps support beta-propeller proteins and explore their roles in sialidases, glycoside hydrolases, and receptors.
YWTD repeats are protein sequence motifs that form six-bladed beta-propeller domains. Found in proteins such as the LDL receptor, these structures help regulate molecular interactions, receptor recycling, and cholesterol uptake.
RCC1 repeats form a distinctive beta-propeller structure in the RCC1 protein. This domain helps regulate Ran, a small GTP-binding protein involved in nuclear transport, chromosome organization, and cell division.
Pumilio repeats, also known as PUF repeats, form RNA-binding protein domains that recognize specific RNA sequences. These proteins regulate gene expression by influencing messenger RNA stability, translation, and other processes involved in cell development and function.
Pentatricopeptide repeats (PPRs) are small protein motifs that form RNA-binding proteins. Found especially in plants, these proteins help regulate RNA editing, stability, splicing, and gene expression in mitochondria and chloroplasts.
Spectrin repeats are structural protein domains made of three alpha helices. They help organize the cytoskeleton, support cell shape, and maintain the stability of cell membranes, particularly in red blood cells and muscle cells.
Leucine-rich repeats (LRRs) are protein structural units that form curved domains for molecular recognition. They play important roles in immune defense, cell signaling, cell adhesion, and the development of tissues and the nervous system.
Kelch repeats are protein structural units that form beta-propeller domains. They help proteins recognize specific partners and play important roles in protein degradation, cellular stress responses, and cytoskeletal organization.
Armadillo repeats are protein structural units made of three alpha helices. They help proteins bind specific partners and play important roles in cell adhesion, nuclear transport, Wnt signaling, and gene regulation.
HEAT repeats are structural units made of alpha helices that help proteins interact with one another. Discover their structure and roles in cellular transport, signaling, metabolism, and protein complex assembly.
WD40 repeat proteins commonly form seven-bladed beta-propellers that function as versatile platforms for protein interactions, signaling, transcription, protein degradation, and cellular regulation.
Beta-propeller proteins can be classified by blade number, sequence repeats, structural features, and biological function. Explore four-, five-, six-, seven-, and eight-bladed beta-propellers, WD40 and Kelch proteins, and important examples.
The beta-propeller is a distinctive protein fold formed by multiple beta-sheet blades arranged around a central axis. Learn how its blades, loops, hydrogen bonds, and central region determine its structure and function.
A beta-propeller is a versatile protein fold composed of multiple beta-sheet blades arranged around a central axis. Learn about its structure, types, functions, evolution, and role in enzymes and protein–protein interactions.
PQQ repeats are protein sequence motifs associated with beta-propeller structures in several enzyme families. Learn how these repeats help organize protein architecture and support the function of PQQ-dependent enzymes, including methanol dehydrogenase.
Asp-box repeats are short sequence and structural motifs found in several protein families. Learn how their beta-hairpin structure helps support beta-propeller proteins and explore their roles in sialidases, glycoside hydrolases, and receptors.
YWTD repeats are protein sequence motifs that form six-bladed beta-propeller domains. Found in proteins such as the LDL receptor, these structures help regulate molecular interactions, receptor recycling, and cholesterol uptake.
RCC1 repeats form a distinctive beta-propeller structure in the RCC1 protein. This domain helps regulate Ran, a small GTP-binding protein involved in nuclear transport, chromosome organization, and cell division.
Pumilio repeats, also known as PUF repeats, form RNA-binding protein domains that recognize specific RNA sequences. These proteins regulate gene expression by influencing messenger RNA stability, translation, and other processes involved in cell development and function.
Pentatricopeptide repeats (PPRs) are small protein motifs that form RNA-binding proteins. Found especially in plants, these proteins help regulate RNA editing, stability, splicing, and gene expression in mitochondria and chloroplasts.
Spectrin repeats are structural protein domains made of three alpha helices. They help organize the cytoskeleton, support cell shape, and maintain the stability of cell membranes, particularly in red blood cells and muscle cells.
Leucine-rich repeats (LRRs) are protein structural units that form curved domains for molecular recognition. They play important roles in immune defense, cell signaling, cell adhesion, and the development of tissues and the nervous system.
Kelch repeats are protein structural units that form beta-propeller domains. They help proteins recognize specific partners and play important roles in protein degradation, cellular stress responses, and cytoskeletal organization.
Armadillo repeats are protein structural units made of three alpha helices. They help proteins bind specific partners and play important roles in cell adhesion, nuclear transport, Wnt signaling, and gene regulation.
HEAT repeats are structural units made of alpha helices that help proteins interact with one another. Discover their structure and roles in cellular transport, signaling, metabolism, and protein complex assembly.
