Peitsch M C, Jongeneel C V
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
Int Immunol. 1993 Feb;5(2):233-8. doi: 10.1093/intimm/5.2.233.
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 alpha 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 TNF beta and comparing it to its crystallographically determined structure. The CD40L sequence is entirely compatible with the 'jelly-roll' beta-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.
基于新鉴定的CD40配体(CD40L)与肿瘤坏死因子(TNFs)在一级结构上的相似性,我们构建了CD40L详细的三维结构模型。我们以肿瘤坏死因子α的已知结构为模板来生成CD40L模型。通过构建肿瘤坏死因子β的三维模型并将其与晶体学确定的结构进行比较,验证了模型构建算法的合理性。CD40L序列与肿瘤坏死因子特有的“果冻卷”β链结构完全兼容。与肿瘤坏死因子一样,预计CD40L会形成紧密的三聚体,尽管单体之间的相互作用与肿瘤坏死因子中的不同。该模型预测了CD40L的哪些区域可能与其受体相互作用,以及哪些氨基酸对于维持其三聚体结构至关重要。