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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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相关实验视频

Updated: Jun 7, 2025

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

12.4K

产生和验证可再生的affimer蛋白结合试剂,针对SH2域.

Sophie J Heseltine1, Gregory J Billenness1, Heather L Martin1

  • 1School of Molecular and Cellular Biology, University of Leeds, Leeds, UK.

Scientific reports
|November 16, 2024
PubMed
概括

研究人员开发了新的affimer试剂,以准特定的sh2域,在癌症等疾病中至关重要. 这些工具使新的查方法成为可能,并显示出开发特定领域抑制剂的潜力.

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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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相关实验视频

Last Updated: Jun 7, 2025

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

12.4K
Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

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科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 药物发现 药物发现 药物发现

背景情况:

  • SH2域对癌症等疾病中涉及的蛋白相互作用至关重要.
  • 现有的研究工具缺乏针对单个SH2域的细胞内测试的特异性.
  • 强化剂试剂为域特定向提供了潜力,但它们对SH2域家族的应用尚未得到充分探索.

研究的目的:

  • 为了识别选择性地与SH2域结合的affimer试剂.
  • 评估这些Affimers在中等通量选中的实用性.
  • 评估affimers作为SH2-介导相互作用的域特异性抑制剂的潜力.

主要方法:

  • 针对41个SH2域的affimer试剂的选择.
  • 开发一个中等通量选试验.
  • 阿菲默结合亲缘关系和抑制潜力的表征.
  • 核转位pERK核转位的阿菲默介导抑制的评估.
  • 在细胞溶解物中对内源Grb2结合的affimer的验证.

主要成果:

  • 识别了能够选择性地结合41个SH2域中的22个的affimer试剂.
  • 在中等通量选方法中证明了affimers的实用性.
  • 展示了以affimer为媒介的pERK核转位的抑制,针对Grb2.
  • 由270.9nM至1.22μM的IC50s和低纳米分子结合亲和度的Grb2特异性强化剂进行量化的竞争性抑制.
  • 证实了Affimers从细胞溶解物中沉内源Grb2的能力.

结论:

  • 可以开发 Affimer 试剂作为 SH2 域的域特异性抑制剂.
  • 这些Affimers是中/高通量表型查的有效工具.
  • 该研究强调了一种有希望的策略,用于识别和表征SH2域家族内的新药标.