McLeary, Darius Clifford James (2017) An investigation of the structure of tumour necrosis factor α in Cyprinus carpio. Masters thesis, Keele University.

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Tumour necrosis factor α (TNF-α) is a soluble cytokine that has a number of different roles in the immune system. It carries out these functions by binding to one of its receptors TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Cyprinus carpio (common carp) is an economically important fish found in Europe and East Asia. Although TNF-α has been found to affect the immune system, its exact structure and function is not known. Knowledge of the structure could help in research into the function of TNF-α in common carp and fish in general.
The four isoforms of TNF-α in common carp are all highly conserved in amino acid sequence when aligned with each other, suggesting a very similar structure and function. TNF-α4 had an extended protein sequence at the C-terminal end, however, this did not affect the alignment. When aligned with TNF-α from humans and mice, several conserved residues were found to affect structure and function in human TNF-α. This was also seen in the alignment of TNF-α from common carp with other species of fish and mammals. A clustering of conserved residues, where structural elements of TNF-α of humans existed, was also observed. The prediction of secondary structure in TNF-α of common carp was very similar to that of TNF-α in humans and mice. The size, position and number of β-strands in the predicted structure was similar to the known structures. However, no α-helices had been predicted, other than in TNF-α4. These results may contribute to the determination of the structure of TNF-α in common carp, which can lead to further research into its function in fish.

Item Type: Thesis (Masters)
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Natural Sciences > School of Life Sciences
Contributors: Shrive, AK (Thesis advisor)
Depositing User: Lisa Bailey
Date Deposited: 20 Nov 2020 17:03
Last Modified: 20 Nov 2020 17:03

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