Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin.
摘要：
Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel β-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.
展开
DOI：
10.1126/science.1709301
被引量：
年份：
1991
万方医学
dx.doi.org
NCBI
Europe PMC
JSTOR
查看更多
NCBI
adsabs.harvard.edu
ProQuest
ResearchGate
ResearchGate
(全网免费下载)
EBSCO
pdb.org
sciencemag.org
mbio.asm.org
mendeley.com
mysciencework.com
www.socolar.com
highbeam.com
go.galegroup.com
scripts.iucr.org
darchive.mbl.edu
embor.embopress.org
plantphysiol.org
rcsb.org
ganino.com
(全网免费下载)
ResearchGate
(全网免费下载)
ganino.com
(全网免费下载)
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！
