3kff | pdb_00003kff

Major mouse urinary protein IV complexed with 2-sec-butyl-4,5-dihydrothiazole

spinqualitylabelsall models 3kff, resolution 0.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kff is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, XBT, ZBT Related: 3kfg, 3kfh, 3kfi Gene: Mup4 (Mus musculus) Resources: FirstGlance, OCA, RCSB, PDBsum Function [MUP4_MOUSE] Binds pheromones, likely to displace pheromones complexed to urinary MUPs and transport them to the vomeronasal organ (VNO) where they associate with their neuronal receptor(s). MUP4 is highly specific for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT). 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 In mice, the major urinary proteins (MUP) play a key role in pheromonal communication by binding and transporting semiochemicals. MUP-IV is the only isoform known to be expressed in the vomeronasal mucosa. In comparison to the MUP isoforms that are abundantly excreted in the urine, MUP-IV is highly specific for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT). In order to examine the structural basis of this ligand preference, we determined the X-ray crystal structure of MUP-IV bound to three mouse pheromones: SBT, 2,5-dimethylpyrazine (DMP), and 2-heptanone (HT). We also obtained the structure of MUP-IV with 2-ethylhexanol bound in the cavity. These four structures show that, relative to the major excreted MUP isoforms, three amino acid substitutions within the binding calyx impact ligand coordination. The F103 for A along with F54 for L result in a smaller cavity, potentially creating a more closely packed environment for the ligand. The E118 for G substitution introduces a charged group into a hydrophobic environment. The sidechain of E118 is observed to hydrogen-bond to polar groups on all four ligands with nearly the same geometry as seen for the water-mediated hydrogen bond network in the MUP-I and MUP-II crystal structures. These differences in cavity size and interactions between the protein and ligand are likely to contribute to the observed specificity of MUP-IV. High resolution X-ray structures of mouse major urinary protein nasal isoform in complex with pheromones.,Perez-Miller S, Zou Q, Novotny MV, Hurley TD Protein Sci. 2010 May 27. PMID:20509168 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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