Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains.
Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains.
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DOI:
10.1073/pnas.83.3.742
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发表时间:
1986-02
影响因子:
11.1
通讯作者:
J. Novotný;S. Tonegawa;H. Saito;D. Kranz;H. Eisen
中科院分区:
文献类型:
--
作者:
J. Novotný;S. Tonegawa;H. Saito;D. Kranz;H. Eisen
To explore the possibility that the difference in antigen recognition between B and T cells derives from a structural difference in their respective antigen-specific receptors (immunoglobulins on B cells and immunoglobulin-like molecules on T cells), we compared the extracellular segments of the T-cell receptor alpha, beta, and gamma polypeptide chains and the N-terminal segment of the T-cell T8 (Lyt-2) antigen chain with the corresponding regions of immunoglobulins whose three-dimensional structures are known. The results indicate that the four T-cell polypeptide chains are organized into immunoglobulin-like domains consisting of multistranded antiparallel beta-sheet bilayers. Invariant amino acid side chains that are conserved in diverse immunoglobulins, including those that mediate domain-domain interactions and form a constant scaffold for antibody binding sites, are also conserved in the chains encoded by the T-cell receptor genes and in the N-terminal domain of T8 (Lyt-2). It appears that the binding sites of the antigen-specific T-cell alpha beta-chain receptors and of antibodies are very similar in their overall dimensions and geometry: a T-cell alpha beta receptor molecule probably has an antigen-specific binding site that is fundamentally no different than the conventional binding site of an antibody.