| 词条 | CRAL-TRIO domain |
| 释义 |
| Symbol = CRAL_TRIO | Name = CRAL/TRIO domain | image =1r5l_opm.png | width =200 | caption = Alpha-tocopherol transfer protein, closed state with ligand.[1] | Pfam= PF00650 | InterPro= IPR001251 | SMART= Sec14 | Prosite = | SCOP = 1aua | TCDB = | OPM family= 121 | OPM protein= 1r5l | CDD = cd00170 | PDB= | Membranome superfamily = 576 }} CRAL-TRIO domain is a protein structural domain that binds small lipophilic molecules.[2] This domain is named after cellular retinaldehyde-binding protein (CRALBP) and TRIO guanine exchange factor. CRALB protein carries 11-cis-retinol or 11-cis-retinaldehyde. It modulates interaction of retinoids with visual cycle enzymes. TRIO is involved in coordinating actin remodeling, which is necessary for cell migration and growth. Other members of the family are alpha-tocopherol transfer protein and phosphatidylinositol-transfer protein (Sec14). They transport their substrates (alpha-tocopherol and phosphatidylinositol or phosphatidylcholine, respectively) between different intracellular membranes. Family also include a guanine nucleotide exchange factor that may function as an effector of RAC1 small G-protein. The N-terminal domain of yeast ECM25 protein has been identified as containing a lipid binding CRAL-TRIO domain.[3] StructureThe Sec14 protein was the first CRAL-TRIO domain for which the structure was determined.[4] The structure contains several alpha helices as well as a beta sheet 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 binding. Human proteins containing this domainC20orf121; MOSPD2; PTPN9; RLBP1; RLBP1L1; RLBP1L2; SEC14L1; SEC14L2; SEC14L3; SEC14L4; TTPA; References1. ^{{cite journal |vauthors=Min KC, Kovall RA, Hendrickson WA |title=Crystal structure of human alpha-tocopherol transfer protein bound to its ligand: implications for ataxia with vitamin E deficiency |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue=25 |pages=14713–8 |date=December 2003 |pmid=14657365 |pmc=299775 |doi=10.1073/pnas.2136684100 |url=}} 2. ^{{cite journal |vauthors=Panagabko C, Morley S, Hernandez M |title=Ligand specificity in the CRAL-TRIO protein family |journal=Biochemistry |volume=42 |issue=21 |pages=6467–74 |date=June 2003 |pmid=12767229 |doi=10.1021/bi034086v |url=|display-authors=etal}} 3. ^{{cite journal |vauthors=Gallego O, Betts MJ, Gvozdenovic-Jeremic J |title=A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae |journal=Mol. Syst. Biol. |volume=6 |issue= 1|pages=430 |date=November 2010 |pmid=21119626 |pmc=3010107 |doi=10.1038/msb.2010.87 |url=|display-authors=etal}} 4. ^{{cite journal |vauthors=Sha B, Phillips SE, Bankaitis VA, Luo M |title=Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein |journal=Nature |volume=391 |issue=6666 |pages=506–10 |date=January 1998 |pmid=9461221 |doi=10.1038/35179 |url=}} External links
3 : Peripheral membrane proteins|Protein domains|Water-soluble transporters |
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