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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment.
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Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment.

机译：人CD3-ε/δ二聚体与UCHT1单链抗体片段复合的晶体结构。

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摘要

The alpha/beta T cell receptor complex transmits signals from MHC/peptide antigens through a set of constitutively associated signaling molecules, including CD3-epsilon/gamma and CD3-epsilon/delta. We report the crystal structure at 1.9-A resolution of a complex between a human CD3-epsilon/delta ectodomain heterodimer and a single-chain fragment of the UCHT1 antibody. CD3-epsilon/delta and CD3-epsilon/gamma share a conserved interface between the Ig-fold ectodomains, with parallel packing of the two G strands. CD3-delta has a more electronegative surface and a more compact Ig fold than CD3-gamma; thus, the two CD3 heterodimers have distinctly different molecular surfaces. The UCHT1 antibody binds near an acidic region of CD3-epsilon opposite the dimer interface, occluding this region from direct interaction with the TCR. This immunodominant epitope may be a uniquely accessible surface in the TCR/CD3 complex, because there is overlap between the binding site of the UCHT1 and OKT3 antibodies. Determination of the CD3-epsilon/delta structure completes the set of TCR/CD3 globular ectodomains and contributes information about exposed CD3 surfaces.
机译：α/βT细胞受体复合物通过一组组成性相关的信号分子，包括CD3-ε/γ和CD3-ε/δ，传递MHC /肽抗原的信号。我们报告了人类CD3-ε/δ胞外域异二聚体和UCHT1抗体的单链片段之间的复合物的1.9-A分辨率的晶体结构。 CD3-ε/δ和CD3-ε/γ在Ig折叠胞外域之间具有保守的界面，两条G链平行堆积。 CD3-δ具有比CD3-γ更负电的表面和更紧密的Ig折叠；因此，两种CD3异二聚体具有明显不同的分子表面。 UCHT1抗体与二聚体界面相反的CD3-ε酸性区域结合，从而阻止了与TCR的直接相互作用。由于UCHT1和OKT3抗体的结合位点之间存在重叠，因此该免疫优势表位可能是TCR / CD3复合物中唯一可访问的表面。 CD3-ε/δ结构的确定完成了TCR / CD3球形胞外域的设置，并提供了有关暴露的CD3表面的信息。

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