University of Tasmania
Browse

File(s) not publicly available

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, JS
The 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.

History

Publication title

Journal of Biological Chemistry

Volume

280

Issue

11

Pagination

10149-10155

ISSN

0021-9258

Department/School

School of Health Sciences

Publisher

Amer Soc Biochemistry Molecular Biology Inc

Place of publication

9650 Rockville Pike, Bethesda, USA, Md, 20814-3996

Repository Status

  • Restricted

Socio-economic Objectives

Clinical health not elsewhere classified

Usage metrics

    University Of Tasmania

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC