1fel

CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN

spinqualitylabelsall models 1fel, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fel is a 1 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FEN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RET4_BOVIN] Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. 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 The three-dimensional structures of complexes between bovine plasma retinol-binding protein (RBP) and three retinol analogs with different end groups (fenretinide, all-trans retinoic acid, and axerophthene) have been determined to 1.8-1.9-A resolution. Their models are very similar to that of the bovine retinol.RBP complex: the root mean square deviations between equivalent alpha-carbons in the two proteins range from 0.17 to 0.24 A. The retinoid molecules fit in the beta-barrel cavity assuming the same conformation of the vitamin, and the substitutions have no consequences on the overall protein structure. While confirming that an intact hydroxyl end group is not an absolute requirement for a correct retinoid binding to RBP, this study has shown the occurrence of conformational changes, although limited, in the rather flexible loop region at the entrance of the beta-barrel upon fenretinide and retinoic acid binding. These changes are suitable for accommodating the end groups of the above retinoids. Instead, no such changes have been revealed in RBP complexed with axerophthene, a retinol analog bearing a hydrogen atom in place of the hydroxyl end group. The protein conformational changes in the above loop region, the steric hindrance of bulky end groups of bound retinoids, and the lack of the retinol hydroxyl group appear to be responsible for the possible reduced affinity of retinoids for RBP relative to retinol and, at the same time, for the abolished or reduced affinity of retinoid.RBP complexes for transthyretin relative to retinol-RBP. Crystallographic studies on complexes between retinoids and plasma retinol-binding protein.,Zanotti G, Marcello M, Malpeli G, Folli C, Sartori G, Berni R J Biol Chem. 1994 Nov 25;269(47):29613-20. PMID:7961949 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinol-binding protein

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