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Binding Stoichiometry of the Cytotoxic T Lymphocyte-associated Molecule-4 (CTLA-4)

Autor: Gina Leytze, Steven G. Nadler, Alison R. Malacko, Peter S. Linsley, Helios T. Leung, Jeff Bradshaw, Mark R. Stebbins, Robert J. Peach, Hans Marquardt, William E. Brady, Shyh Yu Shaw, Jürgen Bajorath, Julie Rogers

Publikováno v: Journal of Biological Chemistry. 270:15417-15424

CD28 and CTLA-4 are homologous T cell receptors of the immunoglobulin (Ig) superfamily, which bind B7 molecules (CD80 and CD86) on antigen-presenting cells and transmit important costimulatory signals during T cell activation. Here we have investigat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c68c4aa830c35118d5d4e5df81b8543e
https://doi.org/10.1074/jbc.270.25.15417

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Complementarity determining region 1 (CDR1)- and CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1

Autor: Naemura Joseph R, William E. Brady, Peter S. Linsley, Gina Leytze, R. Peach, JoAnne L. Greene, Jürgen Bajorath

Publikováno v: The Journal of Experimental Medicine

T cell surface receptors CD28 and CTLA-4 are homologous members of the immunoglobulin superfamily (IgSF), each comprising a single V-like extracellular domain. CD28 and CTLA-4 bind to the B7-1 and B7-2 counter-receptors on antigen presenting cells (A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be24cd39e5980519e27f984df11483c2
http://europepmc.org/articles/PMC2191786

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Activation with superantigens induces programmed death in antigen-primed CD4+ class II+ major histocompatibility complex T lymphocytes via a CD11a/CD18-dependent mechanism

Autor: Kerry Klussman, Nitin K. Damle, Jeffrey A. Ledbetter, Gina Leytze

Publikováno v: European Journal of Immunology. 23:1513-1522

Staphylococcal enterotoxin superantigens (SAg) bind class II major histocompatibility complex (MHC) molecules on antigen-presenting cells (APC) and upon cell-to-cell contact stimulate proliferation of T cells expressing appropriate V beta gene produc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37d5443aca920e22fc8be9c178bcfa7d
https://doi.org/10.1002/eji.1830230718

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Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a clathrin-associated protein is negatively regulated by tyrosine phosphorylation

Autor: Pin Lu, Jeff Bradshaw, Kelly L. Bennett, Stephen E. Kurtz, Julie Rodgers, Peter S. Linsley, Gary L. Schieven, Gina Leytze

Publikováno v: Biochemistry. 36(50)

CTLA-4 (CD152), high-avidity receptor for CD80 and CD86, is a powerful regulator of T cell activation. While CTLA-4 functions at the cell surface, it is primarily localized in intracellular vesicles and cycles to the cell surface. The CTLA-4 cytoplas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53f120178c3ca8590384ec56d3f94deb
https://pubmed.ncbi.nlm.nih.gov/9398332

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Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28

Autor: Keith L. Constantine, Luciano Mueller, Peter S. Linsley, Robert J. Peach, Jürgen Bajorath, Thomas B. Lavoie, William Fenderson, Gina Leytze, William J. Metzler, Shyh Yu Shaw, Naemura Joseph R

Publikováno v: Nature structural biology. 4(7)

The structure of human CTLA-4 reveals that residues Met 99, Tyr 100 and Tyr 104 of the M99YPPPY104 motif are adjacent to a patch of charged surface residues on the A'GFCC' face of the protein. Mutation of these residues, which are conserved in the CT

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::133e3496fe730a479ed75768daded08b
https://pubmed.ncbi.nlm.nih.gov/9228944

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Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions

Autor: John Emswiler, JoAnne L. Greene, Wesley L. Cosand, Jürgen Bajorath, Gina Leytze, Peter S. Linsley, Robert J. Peach

Publikováno v: The Journal of biological chemistry. 271(43)

T lymphocyte receptors CD28 and CTLA-4 bind costimulatory molecules CD80 (B7-1) and CD86 (B7-2) on antigen-presenting cells and regulate T cell activation. While distinct functional roles have been ascribed to each of these molecules, little is known

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::289caf98ccab911c99c14e4793026d94
https://pubmed.ncbi.nlm.nih.gov/8900156

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Both extracellular immunoglobin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28

Autor: Jürgen Bajorath, Alejandro Aruffo, Gina Leytze, Robert J. Peach, JoAnne L. Greene, Naemura Joseph R, Peter S. Linsley

Publikováno v: The Journal of biological chemistry. 270(36)

The B7-related molecules CD80 and CD86 are expressed on antigen-presenting cells, bind the homologous T cell receptors CD28 and CTLA-4, and trigger costimulatory signals important for optimal T cell activation. All four molecules are immunoglobulin s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccb7e580e8ea52f8deac74c1f2ec6499
https://pubmed.ncbi.nlm.nih.gov/7545666

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