Information about Beta Propeller Domain
A beta-propeller domain is an all-β protein fold characterized by 4-8 blade-shaped beta sheets arranged toroidally around a central axis. Each sheet typically has four antiparallel β-strands twisted so that the first and fourth sheets are almost perpendicular to each other. The enzyme's active site is often found in the cleft formed in the center of the propeller by loops connecting the successive four-sheet motifs.
WD40 domains, also known as beta-transducin repeats, are short fragments found in eukaryotes but not in prokaryotes. They are often assembled in 4 to 16 repeated units to form a structural domain for critical for protein-protein interactions.
A structural domain is an element of overall structure within a protein that is self-stabilizing and often folds independently of the rest of the protein chain.
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A structural domain is an element of overall structure within a protein that is self-stabilizing and often folds independently of the rest of the protein chain.
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Examples
The influenza virus protein neuraminidase is a six-bladed beta-propeller protein whose active form is a tetramer. It is one of two proteins present in the viral envelope and catalyzes the cleavage of sialic acid moieties from cell-membrane proteins to aid in the targeting of newly produced virions to previously uninfected cells.WD40 domains, also known as beta-transducin repeats, are short fragments found in eukaryotes but not in prokaryotes. They are often assembled in 4 to 16 repeated units to form a structural domain for critical for protein-protein interactions.
External links
- SCOP 4-bladed beta propellers
- SCOP 5-bladed beta propellers
- SCOP 6-bladed beta propellers
- SCOP 7-bladed beta propellers
- SCOP 8-bladed beta propellers
References
- Branden C, Tooze J. (1999). Introduction to Protein Structure 2nd ed. Garland Publishing: New York, NY.
- Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 371(6495):297-300.
- Smith TF, Gaitatzes C, Saxena K and Neer EJ. (1999) "The WD repeat: a common architecture for diverse functions", TIBS, 24, 181-185.
Protein domains |
|---|
| BZIP - DED - Kringle - PH - SH2 - SH3 - zinc finger - coiled coil - helix bundle - globin fold - twisted open sheet - alpha/beta barrels - up and down barrel - greek key barrel - jelly roll barrel - greek key - leucine-rich repeat - beta propeller - LIM domain - C2 domain |
Protein tertiary structure | |
|---|---|
| General | Structural domain |
| All-α folds: | Helix bundle |
| All-β folds: | Immunoglobulin fold |
| α/β folds: | TIM barrel |
| α+β folds: | Ferredoxin fold |
| Irregular folds: | Conotoxin |
β sheet (also β-pleated sheet) is the second form of regular secondary structure in proteins — the first is the alpha helix — consisting of beta strands
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toroid is a doughnut-shaped object. The surface of such an object is known as a torus. Its annular shape is generated by revolving a circle around an axis external to the circle.
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β sheet (also β-pleated sheet) is the second form of regular secondary structure in proteins — the first is the alpha helix — consisting of beta strands
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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The active site of an enzyme contains the catalytic and binding sites. The structure and chemical properties of the active site allow the recognition and binding of the substrate.
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Influenza
Classification & external resources
TEM of negatively stained influenza virons, magnified approximately 70,000 times
ICD-10 J 10. , J 11.
ICD-9 487
DiseasesDB 6791
MedlinePlus 000080
eMedicine med/1170 ped/3006
MeSH
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Classification & external resources
TEM of negatively stained influenza virons, magnified approximately 70,000 times
ICD-10 J 10. , J 11.
ICD-9 487
DiseasesDB 6791
MedlinePlus 000080
eMedicine med/1170 ped/3006
MeSH
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Neuraminidase is a glycoside hydrolase enzyme (EC 3.2.1.18 ). It is frequently found as an antigenic glycoprotein and is best known as one of the enzymes found on the surface of the Influenza virus.
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A tetramer is a protein with four subunits (tetrameric). There are homo-tetramers (all subunits are identical) such as glutathione S-transferase or single-strand binding protein, dimers of hetero-dimers such as haemoglobin (a dimer of an alpha/beta dimer), and hetero-tetramers,
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viral envelopes covering their protein capsids. The envelopes are typically derived from portions of the host cell membranes (phospholipids and proteins), but include some viral glycoproteins. Functionally, viral envelopes are used to help viruses enter host cells.
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catalysis is the acceleration (increase in rate) of a chemical reaction by means of a substance called a catalyst, which is itself not consumed by the overall reaction.
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Sialic acid is a generic term for the N- or O-substituted derivatives of neuraminic acid, a nine-carbon monosaccharide. It is also the name for the most common member of this group, N-acetylneuraminic acid (Neu5Ac or NANA).
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Prokaryotes (IPA: /prəʊˈkæriəʊtiz/) are a group of organisms that lack a cell nucleus (= karyon), or any other membrane-bound organelles.
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citation, footnoting or external linking.
A structural domain is an element of overall structure within a protein that is self-stabilizing and often folds independently of the rest of the protein chain.
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Protein-protein interactions refer to the association of protein molecules and the study of these associations from the perspective of biochemistry, signal transduction and networks.
The interactions between proteins are important for many biological functions.
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The interactions between proteins are important for many biological functions.
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citation, footnoting or external linking.
A structural domain is an element of overall structure within a protein that is self-stabilizing and often folds independently of the rest of the protein chain.
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Basic Leucine Zipper Domain (bZIP domain) is found in many DNA binding eukaryotic proteins. One part of the domain contains a region that mediates sequence specific DNA binding properties and the Leucine zipper that is required for the dimerization of two DNA binding regions.
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The death-effector domain (DED) is a protein interaction domain found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein (FADD).
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Pleckstrin homology domain (PH domain) is a protein region of approximately 120 amino acids that can bind Phosphatidylinositol lipids within biological membranes (such as Phosphatidylinositol (3,4,5)-trisphosphate and phosphatidylinositol (4,5)-bisphosphate), and proteins such as
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Src homology 2 domain (or SH2 domain) is a protein domain of about 100 amino acid residues first identified as a conserved sequence region among the oncoproteins Src and Fps.
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Src homology 3 domain (or SH3 domain) is a small protein domain of about 60 amino acid residues first identified as a conserved sequence in the non-catalytic part of several cytoplasmic tyrosine kinases such as Abl and Src and it has been then identified in several other
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zinc finger is a protein domain that can bind to DNA. A zinc finger consists of two antiparallel β sheets, and an α helix. The zinc ion is crucial for the stability of this domain type - in absence of the metal ion the domain unfolds as it is too small to have a
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coiled coil is a structural motif in proteins, in which 2-7[1] alpha-helices are coiled together like the strands of a rope (Dimers and trimers are the most common types).
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A helix bundle is a small protein fold composed of three or four alpha helices and held together by nonlocal hydrophobic interactions.
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Three-helix bundles
Three-helix bundles are among the smallest and fastest known cooperatively folding structural domains...... Click the link for more information.
globin fold is a common three-dimensional fold in proteins. This fold typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini.
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TIM barrel is a conserved protein fold consisting of eight α-helices and eight parallel β-strands that alternate along the peptide backbone. The structure is named after triosephosphateisomerase, a conserved glycolytic enzyme.
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Greek key refers to a kind of supersecondary structure or motif of a protein (amino-acid) sequence. It is named for its resemblance to the Greek key meander pattern in art.
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leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold. It is composed of repeating 20-30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine.
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beta-propeller domain is an all-β protein fold characterized by 4-8 blade-shaped beta sheets arranged toroidally around a central axis. Each sheet typically has four antiparallel β-strands twisted so that the first and fourth sheets are almost perpendicular to each other.
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