• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherin.

作者信息

Tong K I, Yau P, Overduin M, Bagby S, Porumb T, Takeichi M, Ikura M

机构信息

Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.

出版信息

FEBS Lett. 1994 Oct 3;352(3):318-22. doi: 10.1016/0014-5793(94)00982-1.

DOI:10.1016/0014-5793(94)00982-1
PMID:7925993
Abstract

Cadherins are a family of Ca(2+)-dependent cell adhesion molecules containing four extracellular tandem repeats each of 110 amino acids. The most amino-terminal repeat is believed to confer the specificity of cell adhesion. A polypeptide containing the amino-terminal repeat of mouse epithelial cadherin has been over-expressed in E. coli and purified to homogeneity. This polypeptide binds Ca2+ with a dissociation constant of 1.6 x 10(-4) M. CD and NMR experiments indicate that the polypeptide adopts a predominantly beta-sheet conformation and that binding of Ca2+ induces only small conformational changes.

摘要

相似文献

1
Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherin.
FEBS Lett. 1994 Oct 3;352(3):318-22. doi: 10.1016/0014-5793(94)00982-1.
2
Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding.钙结合后E-钙黏蛋白重组细胞外结构域的构象变化。
Eur J Biochem. 1994 Aug 1;223(3):1019-26. doi: 10.1111/j.1432-1033.1994.tb19080.x.
3
Calcium binding and homoassociation of E-cadherin domains.E-钙黏蛋白结构域的钙结合与同源缔合
Biochemistry. 1997 Jun 24;36(25):7697-705. doi: 10.1021/bi9705624.
4
Self-assembly of the vascular endothelial cadherin ectodomain in a Ca2+-dependent hexameric structure.
J Biol Chem. 2001 Feb 2;276(5):3581-8. doi: 10.1074/jbc.M002667200. Epub 2000 Nov 7.
5
Calcium-dependent stability studies of domains 1 and 2 of epithelial cadherin.上皮钙黏蛋白结构域1和结构域2的钙依赖性稳定性研究
Biochemistry. 2005 Oct 25;44(42):13692-701. doi: 10.1021/bi0510274.
6
Molecular interactions between desmosomal cadherins.桥粒钙黏蛋白之间的分子相互作用。
Biochem J. 2002 Mar 1;362(Pt 2):317-27. doi: 10.1042/0264-6021:3620317.
7
Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions.通过核磁共振光谱法研究E-钙黏蛋白的钙依赖性同源缔合:迁移率、构象变化及接触区域图谱分析
J Mol Biol. 2002 Dec 6;324(4):823-39. doi: 10.1016/s0022-2836(02)01137-3.
8
Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH: nitrate reductase.菠菜NADH:硝酸还原酶黄素结构域重组形式的光谱和动力学特性
Arch Biochem Biophys. 1996 Mar 1;327(1):151-60. doi: 10.1006/abbi.1996.0103.
9
Interaction of cadmium (Cd(2+)) with a 13-residue polypeptide analog of a putative calcium-binding motif of E-cadherin.
Biochim Biophys Acta. 1999 Aug 12;1451(1):93-100. doi: 10.1016/s0167-4889(99)00077-4.
10
Apoptosis-linked gene product ALG-2 is a new member of the calpain small subunit subfamily of Ca2+-binding proteins.凋亡相关基因产物ALG-2是钙蛋白酶小亚基家族中一种新的钙离子结合蛋白。
Biochemistry. 1999 Jun 8;38(23):7498-508. doi: 10.1021/bi990034n.

引用本文的文献

1
Structure-based models of cadherin-mediated cell adhesion: the evolution continues.基于结构的钙黏蛋白介导的细胞黏附模型:进化仍在继续。
Cell Mol Life Sci. 2004 Aug;61(15):1884-95. doi: 10.1007/s00018-004-4006-2.
2
Cadmium (Cd2+) disrupts E-cadherin-dependent cell-cell junctions in MDCK cells.镉(Cd2+)会破坏MDCK细胞中依赖E-钙黏蛋白的细胞间连接。
In Vitro Cell Dev Biol Anim. 1997 Jul-Aug;33(7):516-26. doi: 10.1007/s11626-997-0094-2.
3
1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin.
J Biomol NMR. 1996 May;7(3):173-89. doi: 10.1007/BF00202035.