Ligand-induced conformational change within the CD2 ectodomain accompanies receptor clustering: Implication for molecular lattice formation
Ligand-induced conformational change within the CD2 ectodomain accompanies receptor clustering: Implication for molecular lattice formation
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DOI:
10.1006/jmbi.1996.0570
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发表时间:
1996-10-25
影响因子:
5.6
通讯作者:
Reinherz, EL
中科院分区:
文献类型:
--
作者:
Li, J;Smolyar, A;Reinherz, EL
CD2 mediates interaction between T cells and their cognate partners through its CD58-binding membrane-distal adhesion domain (D1) facilitating T cell receptor (TCR) triggering. A neoepitope defined by anti-CD2R monoclonal antibodies (mAbs) has suggested structural alteration within the CD2 ectodomain during T cell activation. Here, we map CD2R to the flexible CD2 linker region between D1 and the membrane-proximal extracellular domain (D2) and show that exposure of this conformational site is independent of temperature and metabolic energy. Co-ligation of CD2 and CD58 molecules on opposing cells within a conjugate pair induces CD2R and redistributes CD2 to the region of cell-cell contact. These CD2R(+) molecules, in contrast to the CD2R(-) molecules, are tightly clustered on the T cell surface. Hence, a ligand-mediated increase in the D1-D2 interdomain angle apparently exposes CD2R, facilitates packing of CD2 molecules in a clustered array and is linked to CD2-mediated adhesion and activation events. Conformational alteration of this type may be generally important in ordered lattice formation involving surface receptors. (C) 1996 Academic Press Limited