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| Alpha-tocopherol transfer protein, closed state with ligand | ||
| Identifiers | ||
|---|---|---|
| Symbol | CRAL_TRIO | |
| Pfam | PF00650 | |
| InterPro | IPR001251 | |
| SCOP | 1aua | |
| OPM family | 129 | |
| OPM protein | 1r5l | |
| Available PDB structures:
1aua :108-294 1o6uA:85-244 1olmE:85-244 1r5lA:89-275 1oizA:89-275 1oipA:89-275 |
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CRAL-TRIO domain is a protein structural domain 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 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.
Human proteins containing this domain
C20orf121; MOSPD2; PTPN9; RLBP1; RLBP1L1; RLBP1L2; SEC14L1; SEC14L2; SEC14L3; SEC14L4; TTPA;
References
- [1]. Crystal structure of the Saccharomyces cerevisiae phosphatidyl- inositol-transfer protein. Sha B, Phillips SE, Bankaitis VA, Luo M; Nature 1998;391:506-510. PubMed
External links
- CRAL-TRIO lipid binding domain in PROSITE
- Sec14 domain in SMART
- CRAL/TRIO domain in PFAM
- UMich Orientation of Proteins in Membranes families/superfamily-129 - Calculated spatial positions of CRAL-TRIO domains in membrane
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Wikipedia content modification information:
- This page was last modified on 28 March 2008, at 00:18.
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