2fr3 | pdb_00002fr3

Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 Angstroms Resolution

spinqualitylabelsall models 2fr3, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fr3 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, REA Related: 2fs7, 2frs, 2fru, 2fs6 Gene: CRABP2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [RABP2_HUMAN] Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed CRABPII is a small, cytosolic protein that solubilizes and transfers retinoic acid (RA) to the nucleus while also enhancing its transcriptional activity. We have determined the first high-resolution structure of apo-wild type (WT) CRABPII at 1.35 A. Using three different data sets collected on apo-WT CRABPII we have shown that apo- and holo-CRABPII share very similar structures. Binding of RA appears to increase the overall rigidity of the structure, although the induced structural changes are not as pronounced as previously thought. The enhanced structural rigidity may be an important determinant for the enhanced nuclear localization of the RA-bound protein. Comparison of our apo-WT with a mutant apo-CRABPII structure shows that mutation of Arg111, a conserved residue of CRABPII and a key residue in RA binding, causes structural changes in the molecule. We further investigated the structural importance of conserved residues by determining the structure of the F15W mutant CRABPII (F15W-CRABPII). Our structures also demonstrate structural changes induced by crystal packing and show that a crystal can harbor demonstrative structural differences in the asymmetric unit. The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation.,Vaezeslami S, Mathes E, Vasileiou C, Borhan B, Geiger JH J Mol Biol. 2006 Oct 27;363(3):687-701. Epub 2006 Aug 26. PMID:16979656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CRABP I ( Cellular Retinoic Acid Binding Protein ) Cellular retinoic acid-binding protein Gustavo Elberto Epalza Sanchez/Sandbox 1 Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)

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