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CRAL-TRIO domain is a protein
structural domain In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, thre ...
that binds small lipophilic molecules. This domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor. CRALB protein carries 11-cis-
retinol Retinol, also called vitamin A1, is a fat-soluble vitamin in the vitamin A family that is found in food and used as a dietary supplement. Retinol or other forms of vitamin A are needed for vision, cellular development, maintenance of skin and ...
or 11-cis-retinaldehyde. It modulates interaction of retinoids with visual cycle enzymes. TRIO is involved in coordinating
actin remodeling Actin is a protein family, family of Globular protein, globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in myofibril, muscle fibrils. It is found in essentially all Eukaryote, eukaryotic cel ...
, which is necessary for cell migration and growth. Other members of the family are alpha-
tocopherol Tocopherols (; TCP) are a class of organic compounds comprising various methylated phenols, many of which have vitamin E activity. Because the vitamin activity was first identified in 1936 from a dietary fertility factor in rats, it was named ''t ...
transfer protein and
phosphatidylinositol Phosphatidylinositol or inositol phospholipid is a biomolecule. It was initially called "inosite" when it was discovered by Léon Maquenne and Johann Joseph von Scherer in the late 19th century. It was discovered in bacteria but later also found ...
-transfer protein (Sec14). They transport their substrates ( alpha-tocopherol and
phosphatidylinositol Phosphatidylinositol or inositol phospholipid is a biomolecule. It was initially called "inosite" when it was discovered by Léon Maquenne and Johann Joseph von Scherer in the late 19th century. It was discovered in bacteria but later also found ...
or
phosphatidylcholine Phosphatidylcholines (PC) are a class of phospholipids that incorporate choline as a headgroup. They are a major component of biological membranes and can easily be obtained from a variety of readily available sources, such as egg yolk or soyb ...
, respectively) between different intracellular membranes. Family also include a guanine
nucleotide exchange factor Nucleotide exchange factors (NEFs) are proteins that stimulate the exchange (replacement) of nucleoside diphosphates for nucleoside triphosphates bound to other proteins. Function Many cellular proteins cleave ( hydrolyze) nucleoside triphosphat ...
that may function as an effector of
RAC1 Ras-related C3 botulinum toxin substrate 1, is a protein that in humans is encoded by the ''RAC1'' gene. This gene can produce a variety of alternatively spliced versions of the Rac1 protein, which appear to carry out different functions. Func ...
small
G-protein G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their ...
. The N-terminal domain of yeast ECM25 protein has been identified as containing a lipid binding CRAL-TRIO domain.


Structure

The Sec14 protein was the first CRAL-TRIO domain for which the structure was determined. The structure contains several
alpha helices An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of l ...
as well as a
beta sheet The beta sheet (β-sheet, also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a gene ...
composed of 6 strands. Strands 2,3,4 and 5 form a parallel beta sheet with strands 1 and 6 being anti-parallel. The structure also identified a hydrophobic binding pocket for
lipid Lipids are a broad group of organic compounds which include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E and K), monoglycerides, diglycerides, phospholipids, and others. The functions of lipids include storing ...
binding.


Human proteins containing this domain

C20orf121; MOSPD2; PTPN9; RLBP1; RLBP1L1; RLBP1L2; SEC14L1; SEC14L2; SEC14L3; SEC14L4; TTPA; NF1;


References


External links

* - Calculated spatial positions of CRAL-TRIO domains in membrane Peripheral membrane proteins Protein domains Water-soluble transporters {{membrane-protein-stub