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CD80 binding polyproline helical peptide inhibits T cell activation
journal contribution
posted on 2023-05-17, 05:08 authored by Srinivasan, M, Lu, D, Rajaraman Eri, Brand, DD, Haque, A, Blum, JSThe critical role played by the CD28/CD152-CD80/ CD86 costimulatory molecules in mediating T cell activation and suppression provides attractive targets for therapeutic strategies. CD28 and CD152 share a conserved polyproline motif in the ligand-binding region. Similar proline-rich regions in globular domains preferentially adopt a polyproline type II (PPII) helical conformation and are involved in transient protein-protein interactions. Interestingly, in the human CD80-CD152 complex, Pro102 of CD152 restricts the preceding proline to PPII helix in the binding orientation in relation to the shallow binding pocket of CD80. Peptide agents derived from binding sites of receptors that mimic the bioactive conformation have been shown to block receptor-ligand interactions. Contact preferences of the interface amino acids at the protein-protein interaction sites and the propensity of each residue to form PPII helix were integrated in the design of novel peptide agents referred to as CD80 competitive antagonist peptides. Structural and functional studies suggest potential therapeutic value for select CD80 competitive antagonist peptides. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
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Publication title
Journal of Biological ChemistryVolume
280Issue
11Pagination
10149-10155ISSN
0021-9258Department/School
School of Health SciencesPublisher
Amer Soc Biochemistry Molecular Biology IncPlace of publication
9650 Rockville Pike, Bethesda, USA, Md, 20814-3996Repository Status
- Restricted
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