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The structure of the new DNase was determined
Some Cornell researchers who have long studied proteins are trying to figure out the evolution and operation of proteins by looking at the structural features of proteins. Now, these researchers have identified a crystal structure of a protein (AIRs kinase) that is involved in the production of DNA building blocks. This structure is published in the recent Structure journal. The researchers found that the shape of the AIRs kinase is similar to that of other members of the nucleoside kinase family. This enzyme family is very important in the manufacture of DNA and RNA, and its members are thought to have evolved from a common protein ancestor. So far, the research team has identified nine members of this family. Yan Zhang, a graduate student of Prof. Steven Ealick, succeeded in crystallizing the AIRs kinase protein in only two months. Then we used various advanced technologies to obtain the "optical transform" of this protein. They found that the structure of this kinase is very similar to that of other members of this family of kinases. Ealick speculates that the original enzyme protein plays many roles in cells. In the end, it has evolved and formed a group of different proteins that perform their duties. Ealick's team hopes to be able to design a specific nucleoside kinase and use it as a laboratory tool to detect anticancer drugs and other drugs.
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