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相关概念视频

Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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相关实验视频

Updated: May 9, 2026

Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline
11:09

Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline

Published on: January 5, 2017

Dscam异形特异性的结构基础

Rob Meijers1, Roland Puettmann-Holgado, Georgios Skiniotis

  • 1Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.

Nature
|August 28, 2007
PubMed
概括

唐氏综合症细胞粘附分子 (DSCAM) 基因产生了用于神经元线路的多种受体. 在DSCAM异型中,可变区域通过特定的相互作用来决定同性恋结合特异性.

科学领域:

  • 分子生物学分子生物学
  • 神经科学是一个神经科学.
  • 免疫学 免疫学 免疫学

背景情况:

  • 唐氏综合症细胞粘附分子 (DSCAM) 基因产生了众多细胞表面受体.
  • 这些受体对神经元连接和免疫反应至关重要,提供识别特异性.
  • Dscam的替代拼接会在免疫球蛋白外域 (D2,D3,D7) 中产生序列变异性.

研究的目的:

  • 阐明DSCAM异型识别的结构基础.
  • 研究可变域在同性恋结合特异性中的作用.

主要方法:

  • 进行X射线晶体学以确定DSCAM异型 (D1-D4) 的结构.
  • 结构引导的突变发生和片段交换实验.
  • 对Dscam序列的遗传学分析.

主要成果:

  • 两个不同的DSCAM异型采用了马形的配置.
  • 在D2和D3中的可变残留物形成了两个独立的表面表位 (I和II).
  • 通过涉及表位素I的特定相互作用,DSCAM异构体通过homo-dimerize,可变的段赋予了特异性.

结论:

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  • 以互补的可变残留物为特征的Epitope I对于Dscam同性恋结合特异性至关重要.
  • 遗传学分析支持在表位I中匹配序的强有力的选择.
  • Dscam的同型结合特异性是由表位I内的互补驱动的.