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Ptu1
Ptu1 is a toxin that can reversibly bind N-type calcium channels. It is isolated from the assassin bug ''Peirates turpis''. The toxin belongs to the inhibitory cystine knot structural family (ICK) that has a core of disulfide bonds with four loops emerging from it. Etymology and source Ptu1 is named after the bug ''Peirates turpis'', where it is found. The peptide is found in its saliva. Chemistry and targets Ptu1 is a relatively short peptide of around 3.6 kDa. Its structure belongs to the inhibitory cystine knot family. This is a structural motif that contains at least three disulfide bridges, from which several loops may emerge. The knot is formed by having one disulfide bridge cross the other two disulfide bridges. Disulfide bridges are made by forming a cysteine dimer, called cystine. Due to this, it has a high disulfide content, making ICK motifs highly stable. In line with this, Ptu1 consists of a core of compact disulfide bonds. From this core a total of four loops eme ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Insect Toxins
Insect toxins are various protein toxins produced by insect species. Assassin bugs, sometimes known as kissing bugs, are one of the largest and morphologically diverse families of true bugs feeding on crickets, caterpillars and other insects. Some assassin bug species are bloodsucking parasites of mammals, even feed on humans. They can be commonly found throughout most of the world and their size varies from a few millimeters to as much as 3 or 4 centimeters. The toxic saliva of the predatory assassin bugs contains a complex mixture of small and large peptides for diverse uses such as immobilizing and pre-digesting their prey, as well as defense against competitors and predators. Assassin bug toxins are small peptides with disulfide connectivity that target ion channels. They are relatively homologous to the calcium channel blockers omega-conotoxins from marine cone snails and belong to the four-loop cysteine scaffold structural class. One of these small proteins, Ptu1 Ptu1 is a t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Insect Toxin
Insect toxins are various protein toxins produced by insect species. Assassin bugs, sometimes known as kissing bugs, are one of the largest and morphologically diverse families of true bugs feeding on crickets, caterpillars and other insects. Some assassin bug species are bloodsucking parasites of mammals, even feed on humans. They can be commonly found throughout most of the world and their size varies from a few millimeters to as much as 3 or 4 centimeters. The toxic saliva of the predatory assassin bugs contains a complex mixture of small and large peptides for diverse uses such as immobilizing and pre-digesting their prey, as well as defense against competitors and predators. Assassin bug toxins are small peptides with disulfide connectivity that target ion channels. They are relatively homologous to the calcium channel blockers omega-conotoxins from marine cone snails and belong to the four-loop cysteine scaffold structural class. One of these small proteins, Ptu1 Ptu1 is a t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-type Calcium Channel
N-type calcium channels also called Cav2.2 channels are voltage gated calcium channels that are localized primarily on the nerve terminals and dendrites as well as neuroendocrine cells. The calcium N-channel consists of several subunits: the primary subunit α1B and the auxiliary subunits α2δ and β. The α1B subunit forms the pore through which the calcium enters and helps to determine most of the channel's properties. These channels play an important role in the neurotransmission during development. In the adult nervous system, N-type calcium channels are critically involved in the release of neurotransmitters, and in pain pathways. N-type calcium channels are the target of ziconotide, the drug prescribed to relieve intractable cancer pain. There are many known N-type calcium channel blockers that function to inhibit channel activity, although the most notable blockers are ω-conotoxins. Structure N-type calcium channels are categorized as high threshold-activated channels ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
UniProt
UniProt is a freely accessible database of protein sequence and functional information, many entries being derived from genome sequencing projects. It contains a large amount of information about the biological function of proteins derived from the research literature. It is maintained by the UniProt consortium, which consists of several European bioinformatics organisations and a foundation from Washington, DC, United States. The UniProt consortium The UniProt consortium comprises the European Bioinformatics Institute (EBI), the Swiss Institute of Bioinformatics (SIB), and the Protein Information Resource (PIR). EBI, located at the Wellcome Trust Genome Campus in Hinxton, UK, hosts a large resource of bioinformatics databases and services. SIB, located in Geneva, Switzerland, maintains the ExPASy (Expert Protein Analysis System) servers that are a central resource for proteomics tools and databases. PIR, hosted by the National Biomedical Research Foundation (NBRF) at the Geor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MDPI
MDPI (Multidisciplinary Digital Publishing Institute) is a publisher of open access scientific journals. Founded by Shu-Kun Lin as a chemical sample archive, it now publishes over 390 peer-reviewed, open access journals. MDPI is the largest open access publisher in the world and the fifth largest publisher overall in terms of journal paper output. The number of published papers has been growing significantly in the last decade with year over year growth of over 50% in 2017, 2018 and 2019. As of June 2022, MDPI publishes 393 academic journals, including 93 journals indexed within the Science Citation Index Expanded, and 8 journals indexed within the Social Sciences Citation Index, with a total of 98 journals ranked with an impact factor. MDPI journals are included in the Directory of Open Access Journals. MDPI is a member of the Open Access Scholarly Publishers Association, a participating publisher and supporter of the Initiative for Open Citations, and a member of the Committ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Reduviidae
The Reduviidae are a large cosmopolitan family of the order Hemiptera (true bugs). Among the Hemiptera and together with the Nabidae almost all species are terrestrial ambush predators: most other predatory Hemiptera are aquatic. The main examples of nonpredatory Reduviidae are some blood-sucking ectoparasites in the subfamily Triatominae. Though spectacular exceptions are known, most members of the family are fairly easily recognizable; they have a relatively narrow neck, sturdy build, and a formidable curved proboscis (sometimes called a rostrum). Large specimens should be handled with caution, if at all, because they sometimes defend themselves with a very painful stab from the proboscis. Taxonomy The Reduviidae are members of the suborder Heteroptera of the order Hemiptera. The family members are almost all predatory, except for a few blood-sucking species, some of which are important as disease vectors. About 7000 species have been described, in more than 20 recognized subfa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Inhibitor Cystine Knot
An inhibitor cystine knot (aka ICK or Knottin) is a protein structural motif containing three disulfide bridges. Knottins are one of three folds in the cystine knot motif; the other closely related knots are the Growth Factor Cystine Knot (GFCK) and the Cyclic Cystine Knot (CCK; cyclotide). Types include a) cyclic mobius, b) cyclic bracelet, c) acyclic inhibitor knottins. Cystine knot motifs are found frequently in nature in a plethora of plants, animals, and fungi and serve diverse functions from appetite suppression to anti-fungal activity. Along with the sections of polypeptide between them, two disulfides form a loop through which the third disulfide bond (linking the 3rd and 6th cysteine in the sequence) passes, forming a knot. The motif is common in invertebrate toxins such as those from arachnids and molluscs. The motif is also found in some inhibitor proteins found in plants, but the plant and animal motifs are thought to be a product of convergent evolution. The ICK moti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Disulfide
In biochemistry, a disulfide (or disulphide in British English) refers to a functional group with the structure . The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. In biology, disulfide bridges formed between thiol groups in two cysteine residues are an important component of the secondary and tertiary structure of proteins. ''Persulfide'' usually refers to compounds. In inorganic chemistry disulfide usually refers to the corresponding anion (−S−S−). Organic disulfides Symmetrical disulfides are compounds of the formula . Most disulfides encountered in organo sulfur chemistry are symmetrical disulfides. Unsymmetrical disulfides (also called heterodisulfides) are compounds of the formula . They are less common in organic chemistry, but most disulfides in nature are unsymmetrical. Properties The disulfide bonds are strong, with a typical bond dissociation energy of 60 kcal/mol (251&nbs ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Conotoxin
A conotoxin is one of a group of neurotoxic peptides isolated from the venom of the marine cone snail, genus ''Conus''. Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds. Conotoxins have a variety of mechanisms of actions, most of which have not been determined. However, it appears that many of these peptides modulate the activity of ion channels. Over the last few decades conotoxins have been the subject of pharmacological interest. The LD50 of conotoxin ranges from 5-25 μg/kg. Hypervariability Conotoxins are hypervariable even within the same species. They do not act within a body where they are produced (endogenously) but act on other organisms. Therefore, conotoxin genes experience less selection against mutations (like gene duplication and nonsynonymous substitution), and mutations remain in the genome longer, allowing more time for potentially beneficial novel functions to arise. Variability in c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta Sheet
The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, notably Alzheimer's disease. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A refined versi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
L-type Calcium Channel
The L-type calcium channel (also known as the dihydropyridine channel, or DHP channel) is part of the high-voltage activated family of voltage-dependent calcium channel. "L" stands for long-lasting referring to the length of activation. This channel has four isoforms: Cav1.1, Cav1.2, Cav1.3, and Cav1.4. L-type calcium channels are responsible for the excitation-contraction coupling of skeletal, smooth, cardiac muscle, and for aldosterone secretion in endocrine cells of the adrenal cortex. They are also found in neurons, and with the help of L-type calcium channels in endocrine cells, they regulate neurohormones and neurotransmitters. They have also been seen to play a role in gene expression, mRNA stability, neuronal survival, ischemic-induced axonal injury, synaptic efficacy, and both activation and deactivation of other ion channels. In cardiac myocytes, the L-type calcium channel passes inward Ca2+ current (ICaL) and triggers calcium release from the sarcoplasmic reticul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
P-type Calcium Channel
The P-type calcium channel is a type of voltage-dependent calcium channel. Similar to many other high-voltage-gated calcium channels, the α1 subunit determines most of the channel's properties. The 'P' signifies cerebellar Purkinje cells, referring to the channel's initial site of discovery. P-type calcium channels play a similar role to the N-type calcium channel in neurotransmitter release at the presynaptic terminal and in neuronal integration in many neuronal types. History The calcium channel experiments that led to the discovery of P-type calcium channels were initially completed by Rodolfo Llinas, Llinás and Sugimori in 1980. P type calcium channels were named in 1989 because they were discovered within mammalian Purkinje neurons. They were able to use an ''in vitro'' preparation to examine the ionic currents that account for Purkinje cells' electrophysiology, electrophysiological properties. They found that there are calcium dependent action potentials which rise slowly a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
