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Structural studies on the leukocyte co-stimulatory molecule, B7-1

  • Shinji Ikemizu
  • E. Yvonne Jones
  • David I. Stuart
  • Simon J. Davis
Conference paper

Summary

B7-1 and B7-2 are glycoproteins expressed on antigen presenting cells. The binding of these molecules to the T-cell homodimers, CD28 and CTLA-4, generate ‘costimulatory’ and inhibitory signals in T cells, respectively. The crystal structure of the extracellular region of B7-1 (sB7-l), solved to 3 Å resolution, consists of a novel combination of two Ig-like domains, one characteristic of adhesion molecules and the other previously seen only in antigen receptors. In the crystal lattice, sB7-l unexpectedly forms parallel, 2-fold rotationally symmetric homodimers. The structural data suggest a mechanism whereby the avidity-enhanced binding of B7-1 and CTLA-4 homodimers, along with the relatively high affinity of these interactions, favours the formation of very stable inhibitory signaling complexes.

Key Words

B7-1 CD80 Co-stimulatory molecule Crystal structure 

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Copyright information

© Springer Japan 2001

Authors and Affiliations

  • Shinji Ikemizu
    • 1
  • E. Yvonne Jones
    • 1
    • 2
  • David I. Stuart
    • 1
    • 2
  • Simon J. Davis
    • 3
  1. 1.Division of Structural Biology, Wellcome Trust Centre for Human GeneticsThe University of OxfordOxfordUK
  2. 2.Oxford Centre for Molecular SciencesThe University of Oxford, New Chemistry LaboratoryOxfordUK
  3. 3.Nuffield Department of Clinical MedicineThe University of Oxford, John Radcliffe HospitalHeadingtonUK

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