Nature journal breaks new mechanism of cancer key proteins

A team of researchers from Philadelphia and Norway in the U.S cracked the crystal structure of a key enzyme complex that modifies most human protein ends and presents elevated levels in a variety of cancers The research results are published in the journal Nature Structural & molecular biology The researchers at the Wistar Institute, who led the study, said the findings would help develop inhibitors that inhibit the growth of cancer cells This important protein complex, nata, "seems to be an essential element for cell growth and division, and we have seen an increase in this enzyme in many forms of cancer," article co-author Ronen Dr marmorstein said, "obviously, this is a potential drug target At present, we are developing small molecule drugs that can bind and inhibit Nata through the recent research on this protein." Nata is a member of the N-terminal acetyltransferase (NAT) (or enzyme complex) family It can be used to modify proteins and regulate their behaviors, such as activating proteins, telling them where to move, labeling proteins or for cell degradation Dr marmorstein said Nata has a surprising amino acid sequence specificity, and it would be helpful for drug development to unravel the reason for this specificity "Protein structural modification is a way for cells to regulate protein function," marmorstein explained "Enzymes in the NAT family can modify nearly 85% of human proteins, and 50% of them are completed by these NATAS." Dr marmorstein said that Nata and another protein form a protein complex (one is an enzyme subunit and the other is an auxiliary protein) When researchers use X-ray to construct Nata structure, they found the mechanism of how the auxiliary protein helps the activation of the enzyme subunit The combination of these two proteins will lead to the structural change of enzyme subunits, and make the active sites of the proteins rationally allocated, thus catalyzing the reaction "When an enzyme binds to a helper protein, the Catalytical subunit of Nata actually changes shape and reconfigures its structure to capture the N-terminal sequence of the target protein," marmorstein said At present, scientists have found that the function of Nata is very important for the proliferation of cancer cells, marmorstein said, so understanding Nata structure can help better understand the inactivation mechanism of this protein in cancer cells.