2cbr

CELLULAR RETINOIC ACID BINDING PROTEIN I IN COMPLEX WITH A RETINOBENZOIC ACID (AM80)

spinqualitylabelsall models 2cbr, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cbr is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: A80 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RABP1_BOVIN Cytosolic CRABPs may regulate 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 Retinoids play important roles in diverse cellular processes including growth, cell differentiation and vision. Many natural and synthetic retinoids are used as drugs in dermatology and oncology. A large amount of data has been accumulated on the cellular activity of different synthetic retinoids. They are stabilized and transported inside the cell cytoplasm by binding and transport proteins, such as cellular retinol-binding proteins and cellular retinoic acid binding proteins (CRABPs). The structures of human CRABP II in complex with two different synthetic retinoids, Ro13-6307 and Ro12--7310 (at 2.1 and 2.0 A resolution, respectively) and of bovine CRABP I in complex with a retinobenzoic acid, Am80 (at 2.8 A resolution) are described. The binding affinities of human CRABP I and II for the retinoids studied here have been determined. All these compounds have comparable binding affinities (nanomolar range) for both CRABPs. Apart from the particular interactions of the carboxylate group of the retinoids with specific protein groups, each structure reveals characteristic interactions. Studying the atomic details of the interaction of retinoids with retinoid-binding proteins facilitates the understanding of the kinetics of retinoid trafficking inside the cytoplasm. Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids.,Chaudhuri BN, Kleywegt GJ, Broutin-L'Hermite I, Bergfors T, Senn H, Le Motte P, Partouche O, Jones TA Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1850-7. PMID:10531482 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 3D structures Gustavo Elberto Epalza Sanchez/Sandbox 1 Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)

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