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A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors

Peitsch, Manuel C. ; Jongeneel, C. Victor

In: International Immunology, 1993, vol. 5, no. 2, p. 233-238

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    Titre
    • A 3-D model for the CD40 ligand predicts that it is a compact trimer similar to the tumor necrosis factors
    Auteur
    • Peitsch, Manuel C.. Institute of Biochemistry, University of Lausanne, chemin des Boveresses 155, CH-1066 Epalinges, Switzerland, chemin des Boveresses 155, CH-1066 Epalinges, Switzerland
    • Jongeneel, C. Victor. Ludwig Institute for Cancer Research, Lausanne Branch chemin des Boveresses 155, CH-1066 Epalinges, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • International Immunology, 1993, vol. 5, no. 2, p. 233-238. Oxford University Press
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:293043
    Summary
    Based on the similarity in primary structure between the newly characterized ligand for CD40 (CD40L) and the tumor necrosis factors (TNFs), we have modeled a detailed 3-D structure for CD40L. We used the known structure of TNFα as a template for the generation of the CD40L model. The soundness of the model-building algorithms was verified by constructing a 3-D model of TNFβ and comparing it to its crystallographically determined structure. The CD40L sequence is entirety compatible with the ‘Jelly-roll' β-strand structure characteristic of the TNFs. Like the TNFs, CD40L is predicted to form a compact trimer, although the interactions between monomers are distinct from those found in the TNFs. The model predicts which regions of CD40L could interact with its receptor(s) and which amino acids are essential for the maintenance of its trimeric structure