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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 ( Pfam PF00005 ) have two such regions.
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.
While the S6 domain has been agreed upon as the segment acting as this obstruction, its exact mechanism is unknown. Possible explanations include: the S6 segment makes a scissor-like movement allowing ions to flow through, [ 12 ] the S6 segment breaks into two segments allowing of passing of ions through the channel, [ 13 ] or the S6 channel ...
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 ...
They are usually pentameric with each subunit containing 4 transmembrane helices constituting the transmembrane domain, and a beta sheet sandwich type, extracellular, N terminal, ligand binding domain. [6] Some also contain an intracellular domain like shown in the image. The prototypic ligand-gated ion channel is the nicotinic acetylcholine ...
Simple Modular Architecture Research Tool (SMART) is a biological database that is used in the identification and analysis of protein domains within protein sequences. [ 1 ] [ 2 ] SMART uses profile-hidden Markov models built from multiple sequence alignments to detect protein domains in protein sequences.
Schematic diagram of the 2D structure of aquaporin 1 depicting the six transmembrane alpha-helices and the five interhelical loop regions A-E The 3D structure of aquaporin Z highlighting the 'hourglass'-shaped water channel that cuts through the center of the protein. Aquaporin proteins are composed of a bundle of six transmembrane α-helices ...
Within each of the alpha and beta subunits there is a large extracellular domain, a transmembrane domain and a short cytoplasmic domain. [13] The extracellular domain is where the ligand binds through the use of divalent cations. The integrins contain multiple divalent cation binding sites in the extracellular domain [14]). The integrin cation ...