2FS6

Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II At 1.35 Angstroms Resolution

Summary for 2FS6

• Entry DOI: 10.2210/pdb2fs6/pdb
• Related: 2FR3 2FRR 2FRS 2FRU 2FS0 2FS7
• Descriptor: Cellular retinoic acid-binding protein 2, ACETATE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: crabpii, retinoic acid, retinoids, beta barrel, high resolution, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P29373
• Total number of polymer chains: 2
• Total formula weight: 31635.36

Authors

Vaezeslami, S.,Geiger, J.H. (deposition date: 2006-01-21, release date: 2006-09-19, Last modification date: 2024-02-14)

Primary citation

Vaezeslami, S.,Mathes, E.,Vasileiou, C.,Borhan, B.,Geiger, J.H.
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.
J.Mol.Biol., 363:687-701, 2006

PubMed Abstract: 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.

PubMed: 16979656
DOI: 10.1016/j.jmb.2006.08.059

Experimental method

X-RAY DIFFRACTION (1.35 Å)