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Transmembrane Domain Of ABC Transporters
ABC transporter transmembrane domain is the main transmembrane structural unit of ATP-binding cassette transporter proteins, consisting of six alpha helixes that traverse the plasma membrane. Many members of the ABC transporter family () have two such regions. This family appears to correspond to ABC1 by TCDB classification. Subfamilies * Sulphate ABC transporter permease protein 2 * Phosphate transport system permease protein 2 * Phosphonate uptake transporter * Nitrate transport permease * NifC-like ABC-type porter * Phosphate ABC transporter, permease protein PstC * Molybdate ABC transporter, permease protein * Nickel ABC transporter, permease subunit NikB * Nickel ABC transporter, permease subunit NikC * Ectoine/hydroxyectoine ABC transporter, permease protein EhuD * Ectoine/hydroxyectoine ABC transporter, permease protein EhuC Human proteins containing this domain ABCB1; ABCB10; ABCB11; ABCB4; ABCB5; ABCB6; ABCB7; ABCB8; ABCB9; ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domains
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer after ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
