Classification of SK channel
The SK channel family contains 4 members - SK1, SK2, SK3, and SK4.
Tags: Integral membrane proteins, Ion channels, Membrane proteins, Proteins, Transmembrane proteins
Because all proteins belonging to VAMP/synaptobrevin family share common structural feature, they have been classified as R-SNAREs. An alternative classification (v- and t-SNAREs) exists that takes into account origin of synaptobrevin-bearing organelle rather than their structural properties.
Transmembrane ion channel family was defined in InterPro and Pfam as the family of tetrameric sodium, potassium, and calcium ion channels, in which two C-terminal transmembrane helices flank a loop which determines ion selectivity of the channel pore. This large group of ion channels apparently includes families 1.A.1, 1.A.2, 1.A.3, and 1.A.4 of transporter classification. Many eukariotic channels have four additional transmembrane helices (TMH) (Pfam PF00520), whereas a bacterial structure of the protein has only two transmembrane helices that form the tetrameric channel (Pfam PF07885).
Hyperlipidemias are classified according to the Fredrickson classification which is based on the pattern of lipoproteins on electrophoresis or ultracentrifugation.[1] It was later adopted by the World Health Organization (WHO). It does not directly account for HDL, and it does not distinguish among the different genes that may be partially responsible for some of these conditions. It remains a popular system of classification, but is considered dated by many.
Channel blockers are chemical substances, ranging from ions to complex organic molecules, that bind inside the pore of an ion channel and block the flow of ions through that channel. A subset of channel blockers, known as "open channel blockers" have access to their intra-channel binding site only when the channel is in the open configuration (i.e. in the configuration that conducts transmembrane ion flux). Open channel block is characterized by "flickery closings" in single-channel recordings.
Sequence based classification methods have proven to be a powerful way of generating hypotheses for protein function based on sequence alignment to related proteins. The carbohydrate active enzyme database presents a sequence based classification of glycosyltransferases into over 86 families. The same three-dimensional fold is expected to occur within each of the families.[1]
Sequence-based classifications are among the most powerful predictive method for suggesting function for newly sequenced enzymes for which function has not been biochemically demonstrated. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of more than 100 different families[2][3][4]. This classification is available on the CAZy(CArbohydrate-Active EnZymes) web site[5]. The database provides a series of regularly updated sequence based classification that allow reliable prediction of mechanism (retaining/inverting), active site residues and possible substrates. Based on three dimensional structural similarities, the sequence-based families have been classified into 'clans' of related structure. Recent progress in glycosidase
Glycosides are also classified according to the chemical nature of the aglycone. For purposes of biochemistry and pharmacology, this is the most useful classification.
The molecular classification of ?-lactamases is based on the nucleotide and amino acid sequences in these enzymes. To date, four classes are recognised (A-D), correlating with the functional classification. Classes A, C, and D act by a serine-based mechanism, whereas class B or metallo-?-lactamases need zinc for their action[3] "Penicillinase" was discovered in 1940 and re-named Beta-lactamase when the structure of the Beta-lactam ring was finally elucidated.
The T-type calcium channel is a type of voltage-dependent calcium channel. Like the others of this class, the ?1 subunit is the one that determines most of the channel's properties. Along with sodium "funny current," the T-type calcium channel produces the pacemaker potential in the SA node of the heart. T-type calcium channel blockers are used primarily as antiepileptics.
A Calcium channel is an ion channel which displays selective permeabiltiy to calcium ions. It is sometimes synonymous as voltage-dependent calcium channel,[1] although there are also ligand-gated calcium channels.[2]
A Calcium channel is an ion channel which displays selective permeabiltiy to calcium ions. It is sometimes synonymous as voltage-dependent calcium channel,[1] although there are also ligand-gated calcium channels.[2]
Transporter Classification database (or TCDB) is an IUBMB approved classification system for membrane transport proteins including ion channels. This classification system was designed to be analogous to the EC number system for classifying enzymes, but it also uses phylogenetic information. The upper level of classification and a few examples of proteins with known 3D structure: 1. Channels/Pores Voltage-gated ion channel like, including potassium channels KcsA and KvAP, and inward-rectifier potassium ion channel Kirbac [1] Large-conductance mechanosensitive channel, MscL [2] Small-conductance mechanosensitive ion channel (MscS) [3] CorA metal ion transporters [4] Ligand-gated ion channel of neurotransmitter receptors (acetylcholine receptor) [5] Aquaporins [6] Chloride channels [7] Outer membrane auxiliary proteins (polysaccharide transporter)
Roderick MacKinnon commissioned "Birth of an Idea", a 5' (1.50 m) tall sculpture based on the KcsA potassium channel. The artwork contains a wire object representing the pore liner with a blown glass object representing the main cavity of the channel structure.
Potassium channel, subfamily K, member 2, also known as KCNK2, is a human gene.[1] This gene encodes K2P2.1, one of the members of the two-pore-domain background potassium channel protein family. This type of potassium channel is formed by two homodimers that create a channel that leaks potassium out of the cell to control resting membrane potential. The channel can be opened, however, by certain anesthetics, membrane stretching, intracellular acidosis, and heat. Three transcript variants encoding different isoforms have been found for this gene.
Chloride channel 6, also known as CLCN6, is a human gene.[1] The CLCN family of voltage-dependent chloride channel genes comprises nine members (CLCN1-7, Ka and Kb) which demonstrate quite diverse functional characteristics while sharing significant sequence homology. Chloride channel 6 and 7 belong to a subbranch of this family. Chloride channel 6 has four different alternatively spliced transcript variants. This gene is in close vicinity to two other kidney-specific chloride channel genes, CLCNKA and CLCNKB.[1]