2fs6
Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II At 1.35 Angstroms Resolution
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OverviewOverview
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.
About this StructureAbout this Structure
2FS6 is a Single protein structure of sequence from Homo sapiens with CL, ACT and NA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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