Crystal structure of a human CD3-ε/δ dimer in complex with a UCHT1 single-chain antibody fragment
作者： K. L. Arnett , S. C. Harrison , D. C. Wiley
关键词: T-cell receptor 、 Ectodomain 、 Epitope 、 CD3 Complex 、 Stereochemistry 、 T cell receptor complex 、 Binding site 、 Biology 、 CD3 、 Protein structure
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 between human CD3-epsilon/delta ectodomain heterodimer single-chain fragment UCHT1 antibody. share conserved interface Ig-fold ectodomains, with parallel packing two G strands. CD3-delta has more electronegative surface compact Ig fold than CD3-gamma; thus, CD3 heterodimers have distinctly different molecular surfaces. antibody binds near an acidic region CD3-epsilon opposite dimer interface, occluding this direct interaction TCR. This immunodominant epitope may be uniquely accessible in TCR/CD3 complex, because there is overlap binding site OKT3 antibodies. Determination completes globular ectodomains contributes information about exposed
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