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作 者:刘嘉伟 Liu Jiawei(School of Pharmacy,Nanchang University,Nanchang,330000)
机构地区:[1]南昌大学药学院,南昌330000
出 处:《分子植物育种》2023年第7期2230-2235,共6页Molecular Plant Breeding
基 金:江西省自然科学基金项目(20161BAB205281)资助。
摘 要:有机阴离子转运多肽1B1(OATP1B1)是有机阴离子转运多肽OATP超家族的膜转运蛋白,在药物的吸收、分布、代谢、排泄过程中发挥着重要的作用。本研究从美国国立生物技术信息中心(NCBI)数据库中检索OATP1B1膜蛋白的氨基酸序列,运用生物信息学在线分析软件对OATP1B1蛋白的理化性质、保守结构域、跨膜区、信号肽、磷酸化位点、糖基化位点及相互作用蛋白拓扑网络进行了预测分析。结果表明,OATP1B1为疏水性蛋白,分子中存在12个跨膜结构域,无信号肽序列,有多个磷酸化位点和糖基化位点,是高度磷酸化的糖蛋白。蛋白质二级结构软件在线预测显示,无规则卷曲占46.16%,α-螺旋占34.15%,延伸链占17.66%,β-转角占2.03%。对其相互作用蛋白的拓扑网络预测发现,OATP1B1主要参与胆汁酸,胆汁盐,甲状腺激素等的转运,与药物转运进肝细胞密切相关,另外还参与胆汁分泌。本研究可为研究OATP1B1的药物转运、代谢、排泄机制和联合用药提供理论基础。Organic anion transport polypeptide 1B1(OATPIB1)is a membrane transporter of OATP superfamily,which plays an important role in drug absorption,distribution,metabolism and excretion.We retrieved the amino acid sequence of OATP1B1 from National Center for Biotechnology Information(NCBI)database,predicted and analyzed the physicochemical properties,conserved domain,transmembrane region,signal peptide,phosphoryla-tion site,glycosylation site and topological network of interacting proteins of OATPIB1 protein by using bioinfor-matics online analysis software.The results showed that OATP1B1 was a hydrophobic protein with 12 transmem-brane domains,no signal peptide sequence,multiple phosphorylation sites and glycosylation sites.It was a highly phosphorylated glycoprotein.The results of protein secondary structure prediction showed thatα-helix accounted for 34.15%,β-turn accounted for 2.03%,extended chain accounted for 17.66%,and irregular coil accounted for 46.16%.The topological network prediction of its interacting proteins showed that OATP1B1 was mainly involved in the transport of bile acids,bile salts and thyroid hormones,which was closely related to drug transport into hepa-tocytes,and also involved in bile secretion.This study can provide a theoretical basis for the study of drug trans-port,metabolism,excretion mechanism and combination of OATP1B1.
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