期刊
PROTEIN SCIENCE
卷 10, 期 5, 页码 997-1004出版社
WILEY
DOI: 10.1110/ps.52201
关键词
pheromone; crystal structure; lipocalin; binding protein; X-ray crystallography
资金
- NIDCD NIH HHS [DC02418] Funding Source: Medline
- NIDDK NIH HHS [DK54738] Funding Source: Medline
- NIGMS NIH HHS [R29 GM055055, R01 GM055055, GM55055] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据