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A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain.TMDs may consist of one or several alpha-helices or a transmembrane beta barrel.Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues.
For example, the "unfolded" bacteriorhodopsin in SDS micelles has four transmembrane α-helices folded, while the rest of the protein is situated at the micelle-water interface and can adopt different types of non-native amphiphilic structures. Free energy differences between such detergent-denatured and native states are similar to stabilities ...
Metal transporter CNNM3 primary structure. Regarding the structure, CNNMs contain an N-terminal extracellular domain, a transmembrane domain called DUF21, a large cytosolic region that includes a pair of cystathionine-β-synthase domains, known as CBS-pair, and, furthermore, a putative cyclic nucleotide-binding homology domain, which name is CNBH (Cyclic Nucleotide-Binding Homology).
The transmembrane subunit of the vitamin B 12 importer, BtuCD, contains 10 TM helices and the functional unit consists of two copies each of the nucleotide binding domain (NBD) and transmembrane domain (TMD). The TMD and NBD interact with one another via the cytoplasmic loop between two TM helices and the Q loop in the ABC.
This causes the cross-prediction between them, which is a weakness of many transmembrane topology predictors. By predicting signal peptides and transmembrane helices simultaneously (Phobius [14]), the errors caused by cross-prediction are reduced and the performance is substantially increased. Another feature used to increase the accuracy of ...
A cartoon representation of a CLC chloride channel. The arrows indicate the orientation of each half of the individual subunit. Each CLC channel is formed from two monomers, each monomer containing the antiparallel transmembrane domain. Each monomer has its own pore through which chloride and other anions may be conducted.
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Eight transmembrane segments that form a channel and allow for Cu(I) to pass through the membrane; An ATP-binding domain; A large N-terminal cytosolic domain that contains six repeated Cu(I)-binding sites, each containing a GMTCXXC motif. Proposed structure of copper-transporting protein ATP7A. Many motifs in the ATP7A structure are conserved: [11]