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Tumour necrosis factor ligand superfamily member 8 (TNFL8) is a cytokine that plays vital roles in immune activations and inflammatory responses through its interaction with the tumour necrosis factor superfamily member. Despite multiple studies on the involvement of its receptor in the inflammatory response, there is limited information on the molecular characterization and structural elucidation of the cytokine. Considering the significance of the cytokine, the three-dimensional structure of TNFL8 model was generated by homology modelling through the Iterative Threading ASSEmbly Refinement (I-TASSER) server and validated through PROCHECK and Qualitative Model Energy Analysis (QMEAN) servers. The predicted structure has 90.00% of residues in the most favoured region of the Ramachandran plot while the QMEAN value gives − 3.06. The sequence and structural alignment between the generated model of the cytokine and template (1XU2) reveal that similar active site residues such as ILE-142, THR-175, GLU-178, and PHE-228 could be involved in binding pocket formation. However, docking studies of the 3D model of TNFL8 with eight phytochemicals from the extract of Xylopia aethiopica (Dunal) A. Rich revealed the phytochemical bound to two different binding sites which could be the active regions of the cytokine that could be essential for inhibition. More so, the docking analysis showed most of the phytochemicals have good binding affinity to the cytokine with ellagic acid showing the highest affinity with a binding energy of − 6.58 ± 0.18 kcal/mol. The proposed model may shed light on the mechanisms of TNFL8 binding and provide insights into the identification of potential molecular targets for the development of the novel compound for the regulation of the functional activities of the cytokine.

Homology modelling and analysis of structure predictions of human tumour necrosis factor ligand superfamily member 8