Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid Signaling
摘要:
Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.
展开
关键词:
Experimental/ biomembrane transport crystal structure lipid bilayers molecular biophysics molecular configurations proteins/ structural adaptations membrane enzyme endocannabinoid signaling termination chemical messengers amino acids monoamines peptide hormones lipids cellular communication nervous system integral membrane protein fatty acid amide hydrolase discrete structural alterations soluble hydrolases active site/ A8715B Biomolecular structure, configuration, conformation, and active sites A3620H Macromolecular configuration (bonds, dimensions) A8725D Biological transport cellular and subcellular transmembrane physics
DOI:
10.1126/science.1076535
被引量:
年份:
2002

















































通过文献互助平台发起求助,成功后即可免费获取论文全文。
相似文献
参考文献
引证文献
来源期刊
引用走势
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用!