7O0J
High resolution structure of recombinant chichen liver Bile Acid Binding Protein (cL-BABP)
Summary for 7O0J
| Entry DOI | 10.2210/pdb7o0j/pdb |
| Descriptor | Fatty acid-binding protein, liver (2 entities in total) |
| Functional Keywords | fatty acid binding protein, chicken liver bile acid binding protein, recombinant, lipid binding protein |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 14513.65 |
| Authors | Tassone, G.,Pozzi, C. (deposition date: 2021-03-26, release date: 2021-05-12, Last modification date: 2024-01-31) |
| Primary citation | Tassone, G.,Orlandini, M.,Olivucci, M.,Pozzi, C. Validation of Recombinant Chicken Liver Bile Acid Binding Protein as a Tool for Cholic Acid Hosting. Biomolecules, 11:-, 2021 Cited by PubMed Abstract: Bile acids (BAs) are hydroxylated steroids derived from cholesterol that act at the intestinal level to facilitate the absorption of several nutrients and also play a role as signaling molecules. In the liver of various vertebrates, the trafficking of BAs is mediated by bile acid-binding proteins (L-BABPs). The ability to host hydrophobic or amphipathic molecules makes BABPs suitable for the distribution of a variety of physiological and exogenous substances. Thus, BABPs have been proposed as drug carriers, and more recently, they have also been employed to develop innovative nanotechnology and biotechnology systems. Here, we report an efficient protocol for the production, purification, and crystallization of chicken liver BABP (cL-BABP). By means of target expression as His-tag cL-BABP, we obtained a large amount of pure and homogeneous proteins through a simple purification procedure relying on affinity chromatography. The recombinant cL-BABP showed a raised propensity to crystallize, allowing us to obtain its structure at high resolution and, in turn, assess the structural conservation of the recombinant cL-BABP with respect to the liver-extracted protein. The results support the use of recombinant cL-BABP for the development of drug carriers, nanotechnologies, and innovative synthetic photoswitch systems. PubMed: 33925706DOI: 10.3390/biom11050645 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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