1kgl | pdb_00001kgl

Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol

spinqualitylabelsall models 1kgl Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kgl is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: RTL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RET1_RAT Intracellular transport of retinol. 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 Retinoid-binding proteins play an important role in regulating transport, storage, and metabolism of vitamin A and its derivatives. The solution structure and backbone dynamics of rat cellular retinol-binding protein type I (CRBP) in the apo- and holo-form have been determined and compared using multidimensional high resolution NMR spectroscopy. The global fold of the protein is consistent with the common motif described for members of the intracellular lipid-binding protein family. The most relevant difference between the NMR structure ensembles of apo- and holoCRBP is the higher backbone disorder, in the ligand-free form, of some segments that frame the putative entrance to the ligand-binding site. These comprise alpha-helix II, the subsequent linker to beta-strand B, the hairpin turn between beta-strands C and D, and the betaE-betaF turn. The internal backbone dynamics, obtained from 15N relaxation data (T1, T2, and heteronuclear nuclear Overhauser effect) at two different fields, indicate several regions with significantly higher backbone mobility in the apoprotein, including the betaC-betaD and betaE-betaF turns. Although apoCRBP contains a binding cavity more shielded than that of any other retinoid carrier, conformational flexibility in the portal region may assist retinol uptake. The stiffening of the backbone in the holoprotein guarantees the stability of the complex during retinol transport and suggests that targeted retinol release requires a transiently open state that is likely to be promoted by the acceptor or the local environment. Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution.,Franzoni L, Lucke C, Perez C, Cavazzini D, Rademacher M, Ludwig C, Spisni A, Rossi GL, Ruterjans H J Biol Chem. 2002 Jun 14;277(24):21983-97. Epub 2002 Apr 4. PMID:11934897 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Retinol-binding protein 3D structures

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