TIMM, David E., L. J. BAKER, H MUELLER, Lukáš ŽÍDEK and Milos NOVOTNY. Structural basis of pheromone binding to mouse major urinary protein (MUP-I). Protein Science. Plainview: Cold Spring Harbor Lab. Press, 2001, vol. 10, No 5, p. 997-1005. ISSN 0961-8368.
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Basic information
Original name Structural basis of pheromone binding to mouse major urinary protein (MUP-I)
Authors TIMM, David E., L. J. BAKER, H MUELLER, Lukáš ŽÍDEK and Milos NOVOTNY.
Edition Protein Science, Plainview, Cold Spring Harbor Lab. Press, 2001, 0961-8368.
Other information
Type of outcome Article in a journal
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.472
Organization unit Faculty of Science
Keywords in English FEMALE MICE; HOUSE MOUSE; PUBERTY; RESOLUTION; CRYSTALLOGRAPHY; REFINEMENT; LIPOCALIN; MUSCULUS; LIGAND; GENES
Tags CRYSTALLOGRAPHY, FEMALE MICE, GENES, HOUSE MOUSE, LIGAND, LIPOCALIN, MUSCULUS, PUBERTY, REFINEMENT, RESOLUTION
Changed by Changed by: prof. Mgr. Lukáš Žídek, Ph.D., učo 38990. Changed: 21/5/2001 10:01.
Abstract
The mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effecters 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.
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