Structure solved at Scripps shows how one human protein reduces potency of chemotherapy

ested in clinical trials as an adjuvant for chemotherapy. The idea is that these inhibitors could be administered at the same time as chemotherapy to make chemotherapy more effective.

"Having the structure solved allows us to make [inhibitors] that are [even] more selective," Pegg says.

The structure also provides a way of designing proteins to improve cancer treatments, says Tainer. The molecular details of the structure show how AGT could be modified to resist selective inhibitors. This could be used to protect critical tissues from the chemotherapy even when administered at high doses. For example, a cancer patient taking chemotherapy and AGT inhibitors could at the same time receive an infusion of modified bone marrow cells that would have a form of AGT protein able to resist the inhibitors, which could protect the patient from some of chemotherapy's more toxic side effects.

Daniels and Tainer had already solved the free-form structure of AGT (not bound to DNA), and when they compared this to the DNA-bound form, they found that the structures were identical. The fact that AGT's structure does not change after binding the DNA suggests a simple one-step pathway whereby AGT repairs damaged DNA.

The model that Daniels, Tainer, Pegg, and their colleagues are suggesting is one of twist and grab.

AGT recognizes a piece of DNA that is damaged and binds to that DNA. Then it twists out the phosphate backbone of the DNA, exposing the damaged base, repairs the base by grabbing the offending alkyl group and transferring it onto itself, and releases the now repaired section of DNA. In doing so, the protein is used up.

DNA commonly twists in such a way that there is a major groove (like the part of the staircase with the steps) and a minor groove (like the part with the rail). One of the details that has emerged from this study is that AGT recognizes the minor groove of DNA.

Most proteins that bind to DNA bind in

Contact: Jason Bardi
Scripps Research Institute

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