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Antibody Structure01:10

Antibody Structure

60.1K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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Antibody Structure and Classes01:25

Antibody Structure and Classes

901
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Antibody Actions01:26

Antibody Actions

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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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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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Updated: Jul 1, 2025

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
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抗体CDR循环在结合时是否会改变形状?

Chu'nan Liu1, Lilian M Denzler1, Oliver E C Hood1

  • 1Structural and Molecular Biology, Division of Biosciences, University College London, London, UK.

mAbs
|March 13, 2024
PubMed
概括
此摘要是机器生成的。

抗体药物开发需要了解抗原结合. 这项研究分析了抗体结构,发现补充性决定区域 (CDR) 在结合时显示最小的构造变化,除了CDR-H3.

关键词:
在CDR的灵活性和灵活性.这些CDR是CDR.抗体是对抗体的重要组成部分.抗体结合 抗体结合抗体结构 抗体结构互补性决定了地区的互补性.

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科学领域:

  • 结构生物学是结构生物学.
  • 免疫学 免疫学 免疫学
  • 计算化学是一种计算化学.

背景情况:

  • 抗体是关键的治疗药物,有100多种许可药物.
  • 修改抗体亲和力需要了解抗体-抗原相互作用.
  • 在抗原结合时,互补性决定区域 (CDR) 的形状变化仍然是一个悬而未决的问题.

研究的目的:

  • 在抗体-抗原结合过程中进行CDR形状变化的大规模调查.
  • 分析抗原结合对抗体CDR结构的影响.
  • 为改善抗体建模和药物设计提供数据.

主要方法:

  • 从蛋白质数据库中编制了177个抗体的数据集 (AbAgDb),这些抗体具有结合和不结合的结构.
  • 使用RMSD分析分析了CDR中的Cα脊柱形状变化.
  • 将绑定的CDR形态与未绑定的CDR的形态空间进行比较.

主要成果:

  • 大多数CDR,除了CDR-H3,在抗原结合时表现出最小的形状变化.
  • 70.6%和87%的CDR-H3s显示全球Cα RMSD≤1.0Å和≤2.0Å,分别.
  • 大多数绑定的CDR构造在未绑定的CDR构造空间内被发现.

结论:

  • 抗体CDRs,特别是CDR-H3,在结合抗原时经历了有限的形状调整.
  • 现有的未结合的CDR形态数据足够地代表了大多数CDR的结合状态.
  • 这些发现将为抗体建模,对接策略和药物开发提供信息.