title: Validation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations.
abstract: We have calculated proton chemical shift perturbations (CSPs) of retinol in the cellular retinol-binding protein (CRBP) through the use of a recently developed computational approach (Wang et al. J. Chem. Phys. 2004, 120, 11392-11400). Excellent agreement with experimental values was obtained for the X-ray structure, whereas the lack of a key hydrogen bond and the distorted isoprene tail of retinol for some NMR models lead to large CSP RMSDs. Therefore, a comparison of computed CSPs of retinol with experiment offers a convenient way to validate the structure of retinol and its orientation in the binding site for the NMR structures.
authors.affiliation: Department of Chemistry, The Pennsylvania State University, 104 Chemistry Building, University Park, Pennsylvania 16802, USA.
authors.forename: Bing
authors.initials: B
authors.lastname: Wang
authors.forename: Kenneth M
authors.initials: KM
authors.lastname: Merz
mesh_terms: D001665:Binding Sites; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D015203:Reproducibility of Results; D012177:Retinol-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D054840:Retinol-Binding Proteins, Cellular
chemical_list: D008024:Ligands; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular