2nnd | pdb_00002nnd

The Structural Identification of the Interaction Site and Functional State of RBP for its Membrane Receptor

spinqualitylabelsall models 2nnd, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nnd is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, PRZ Related: 2nne Gene: MUP1, Mup2 (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MUP2_MOUSE] Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. 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 This laboratory has advanced a model whereby retinol is transported around the body bound to retinol-binding protein (RBP), is transferred across the membrane of cells by a specific receptor/transporter, and is picked up from the membrane by an intracellular homolog, cellular retinol-binding protein (CRBP). This process involves a number of protein-protein interactions, and we hypothesized that conformational changes were an integral part of the retinol transfer mechanism. Previously we identified the potential interaction site on RBP for its membrane receptor. Here we confirm by the analysis of chimera containing a grafted CD loop from RBP that this is indeed the receptor interaction site and go on to demonstrate that the conformational changes that occur to this region on the apo to holo transition in RBP also take place in a chimera binding a quite different ligand, thus establishing the concept. We have also gone on to support the hypothesis that CRBP may also bind to a receptor in the membrane. Previous evidence has indicated that one such receptor might be lecithin:retinol acyltransferase, an enzyme that catalyzes retinol esterification. Here we provide the first evidence that the plasma membrane receptor for RBP could be the same as that for CRBP. This observation offers support for the intracellular phase of the uptake process for retinol, providing an efficient and highly unique mechanism in eukaryotic biology. Identification of the retinol-binding protein (RBP) interaction site and functional state of RBPs for the membrane receptor.,Redondo C, Vouropoulou M, Evans J, Findlay JB FASEB J. 2008 Apr;22(4):1043-54. Epub 2007 Nov 8. PMID:17991731 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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