Detailed Information on Publication Record
2001
Structural basis of pheromone binding to mouse major urinary protein (MUP-I)
TIMM, David E., L. J. BAKER, H MUELLER, Lukáš ŽÍDEK, Milos NOVOTNY et. al.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
Článek v odborném periodiku
Confidentiality degree
není předmětem státního či obchodního tajemství
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
Změněno: 21/5/2001 10:01, prof. Mgr. Lukáš Žídek, Ph.D.
Abstract
V originále
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.