Abstract
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 α, β, and γ 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 β-sheet bilayers. Invariant amino acid side chains that are conserved in diversed 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 αβ-chain receptors and of antibodies are very similar in their overall dimensions and geometry: a T-cell αβ receptor molecule probably has an antigen-specific binding site that is fundamentally no different than the conventional binding site of an antibody.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 742-746 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 83 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jan 1 1986 |
| Externally published | Yes |
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Cite this
Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains. / Novotný, J.; Tonegawa, S.; Saito, H.; Kranz, D. M.; Eisen, H. N.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 3, 01.01.1986, p. 742-746.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains
AU - Novotný, J.
AU - Tonegawa, S.
AU - Saito, H.
AU - Kranz, D. M.
AU - Eisen, H. N.
PY - 1986/1/1
Y1 - 1986/1/1
N2 - 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 α, β, and γ 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 β-sheet bilayers. Invariant amino acid side chains that are conserved in diversed 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 αβ-chain receptors and of antibodies are very similar in their overall dimensions and geometry: a T-cell αβ receptor molecule probably has an antigen-specific binding site that is fundamentally no different than the conventional binding site of an antibody.
AB - 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 α, β, and γ 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 β-sheet bilayers. Invariant amino acid side chains that are conserved in diversed 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 αβ-chain receptors and of antibodies are very similar in their overall dimensions and geometry: a T-cell αβ receptor molecule probably has an antigen-specific binding site that is fundamentally no different than the conventional binding site of an antibody.
UR - http://www.scopus.com/inward/record.url?scp=0005138727&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0005138727&partnerID=8YFLogxK
U2 - 10.1073/pnas.83.3.742
DO - 10.1073/pnas.83.3.742
M3 - Article
C2 - 3484824
AN - SCOPUS:0005138727
VL - 83
SP - 742
EP - 746
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 3
ER -