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Updated: Jul 21, 2026

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
19:05

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Published on: October 30, 2015

类I重链的诱导的形状变化

T Elliott1, V Cerundolo, J Elvin

  • 1Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, UK.

Nature
|May 30, 1991
PubMed
概括

特定的在I类分子组装中起着双重作用. 它们诱导重链折叠并稳定与β2-微球蛋白的关联,影响免疫反应.

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Antibody Structure01:10

Antibody Structure

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.
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Antibody Structure01:10

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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.
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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.