| Title: | Structural basis of pheromone binding to mouse major urinary protein (MUP-I) |
| Author(s): | Timm DE; Baker LJ; Mueller H; Zidek L; Novotny MV; |
| Address: | "Department of Biochemistry, Indiana University, Indianapolis, Indiana 46202, USA. dtimm@iupui.edu" |
| ISSN/ISBN: | 0961-8368 (Print) 1469-896X (Electronic) 0961-8368 (Linking) |
| Abstract: | "The mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effectors of mouse physiology and behavior. Crystal structures of recombinant mouse major urinary protein-I (MUP-I) complexed with the synthetic pheromones, 2-sec-butyl-4,5-dihydrothiazole and 6-hydroxy-6-methyl-3-heptanone, have been determined at high resolution. The purification of MUP-I from mouse liver and a high-resolution structure of the natural isolate are also reported. These results show the binding of 6-hydroxy-6-methyl-3-heptanone to MUP-I, unambiguously define ligand orientations for two pheromones within the MUP-I binding site, and suggest how different chemical classes of pheromones can be accommodated within the MUP-I beta-barrel" |
| Keywords: | "Animals Binding Sites Crystallography, X-Ray Hydrogen Bonding Liver/chemistry Mice Models, Molecular Pheromones/chemical synthesis/chemistry/*metabolism Protein Binding Protein Structure, Secondary Proteins/*chemistry/*metabolism Structure-Activity Relati;" |
| Notes: | "MedlineTimm, D E Baker, L J Mueller, H Zidek, L Novotny, M V eng R01 GM055055/GM/NIGMS NIH HHS/ GM55055/GM/NIGMS NIH HHS/ DC02418/DC/NIDCD NIH HHS/ DK54738/DK/NIDDK NIH HHS/ R29 GM055055/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 2001/04/24 Protein Sci. 2001 May; 10(5):997-1004. doi: 10.1110/ps.52201" |
