International Immunology, Vol. 5, No. 2, pp. 233-238,February 1993
© 1993 Japanese Society for Immunology
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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
Institute of Biochemistry, University of Lausanne chemin des Boveresses 155, CH-1066 Epalinges, Switzerland
1 Ludwig Institute for Cancer Research, Lausanne Branch chemin des Boveresses 155, CH-1066 Epalinges, Switzerland
Correspondence to: Correspondence to: M. C. Peitsch
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 TNF
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 TNFß and comparing it to its crystallographically determined structure. The CD40L sequence is entirety compatible with the ‘Jelly-roll’ ß-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.
Keywords: antigen activation, antigen differentiation, B lymphocytes, molecular models, T lymphocytes, tumor necrosis factor
Received 13 September 1992, accepted 11 November 1992.
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