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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.
Schematic representation of transmembrane proteins: 1) a single-pass membrane protein 2) a multipass membrane protein (α-helix) 3) a multipass membrane protein β-sheet. The membrane is represented in light yellow. A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane.
Although several protein families have four transmembrane alpha-helices, tetraspanins are defined by conserved amino acid sequences including four or more cysteine residues in the EC2 domain, with two in a highly conserved 'CCG' motif. Tetraspanins are often thought to act as scaffolding proteins, anchoring multiple proteins to one area of the ...
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.
The outer membrane mitochondrial proteins carry out functions for mitochondrial biogenesis and integration between mitochondria and the cellular system. The outer membrane consists of two types of integral proteins, including proteins with transmembrane β-barrel and proteins with one or more α-helical membrane anchors. [5] [6]
A recent review discusses evidence regarding the structure and function of claudin family proteins using a systems approach to understand evidence generated by proteomics techniques. [13] A chimeric claudin was synthesized to help enhance the understanding of both the structure and function of the tight junction. [14]
Transmembrane channels, also called membrane channels, are pores within a lipid bilayer. The channels can be formed by protein complexes that run across the membrane or by peptides . They may cross the cell membrane , connecting the cytosol , or cytoplasm , to the extracellular matrix . [ 1 ]
The protein can broadly be split into the Notch extracellular domain (NECD) and Notch intracellular domain (NICD) joined together by a single-pass transmembrane domain (TM). The NECD contains 36 EGF repeats in Drosophila , [ 13 ] 28-36 in humans, and 13 and 10 in C. elegans Lin-12 and GLP-1 respectively. [ 27 ]