![]() |
|
PROSITE documentation PDOC50191 |
The CRAL-TRIO domain is a structurally conserved element of about 170 amino acids, which constitute a hydrophobic lipid binding pocket. The CRAL-TRIO domain is found in GTPase-activating proteins (GAPs), guanine nucleotide exchange factors (GEFs) and a family of hydrophobic ligand binding proteins, including the yeast SEC14 protein and mammalian retinaldehyde- and α-tocopherol-binding proteins. The CRAL-TRIO domain may either constitute all of the protein or only part of it [1,2,3,4,5].
The resolution of the crystal structure of SEC14 has revealed the structure of the CRAL-TRIO lipid binding domain (see <PDB:1AUA>). The CRAL-TRIO lipid binding domain is an α/β domain, which forms a large hydrophobic pocket. The pocket floor is constituted by six β-strands and the sides of the cavity are formed by α-helices [3].
Some proteins known to contain a CRAL-TRIO domain are listed below:
The profile we developed covers the entire CRAL-TRIO domain.
Last update:June 2002 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Salama S.R. Cleves A.E. Malehorn D.E. Whitters E.A. Bankaitis V.A. |
Title | Cloning and characterization of Kluyveromyces lactis SEC14, a gene whose product stimulates Golgi secretory function in Saccharomyces cerevisiae. | |
Source | J. Bacteriol. 172:4510-4521(1990). | |
PubMed ID | 2198263 |
2 | Authors | Sato Y. Arai H. Miyata A. Tokita S. Yamamoto K. Tanabe T. Inoue K. |
Title | Primary structure of alpha-tocopherol transfer protein from rat liver. Homology with cellular retinaldehyde-binding protein. | |
Source | J. Biol. Chem. 268:17705-17710(1993). | |
PubMed ID | 8349655 |
3 | Authors | Sha B. Phillips S.E. Bankaitis V.A. Luo M. |
Title | Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. | |
Source | Nature 391:506-510(1998). | |
PubMed ID | 9461221 | |
DOI | 10.1038/35179 |
4 | Authors | Aravind L. Neuwald A.F. Ponting C.P. |
Title | Sec14p-like domains in NF1 and Dbl-like proteins indicate lipid regulation of Ras and Rho signaling. | |
Source | Curr. Biol. 9:R195-R197(1999). | |
PubMed ID | 10209105 |
5 | Authors | Zimmer S. Stocker A. Sarbolouki M.N. Spycher S.E. Sassoon J. Azzi A. |
Title | A novel human tocopherol-associated protein: cloning, in vitro expression, and characterization. | |
Source | J. Biol. Chem. 275:25672-25680(2000). | |
PubMed ID | 10829015 | |
DOI | 10.1074/jbc.M000851200 |