Autor: |
Ataur R. Katebi, Pawel Gniewek, Saras Saraswathi, Robert L. Jernigan, Michael T. Zimmermann, Christopher K. Tuggle, Andrzej Kloczkowski, Zhenming Gong |
Rok vydání: |
2010 |
Předmět: |
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Zdroj: |
BCB |
DOI: |
10.1145/1854776.1854902 |
Popis: |
IL1β is an important protein in vertebrates. It is a member of the cytokine protein family and is involved in generating an inflammatory response to infections. Researchers have found that there are two porcine IL1β proteins expressed - one in embryos and the other in macrophage and endometrial tissues. These two proteins have about 86% sequence identity. In this paper, we attempt to describe how these two proteins might differ structurally and functionally. We find that 1) A predicted binding site appears to have different side chain arrangements that might lead to different binding efficiencies for the same protein or even to different partners. 2) The Caspase 1 cleavage site in the precursor proteins differs in a way that has previously been experimentally determined to reduce the cleavage activity by one order of magnitude for the embryonic IL1β, conferring a significant advantage to the protein (embryonic IL1β). |
Databáze: |
OpenAIRE |
Externí odkaz: |
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