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Lead discovery and in silico 3D structure modeling of tumorigenic FAM72A (p17)
Subrata Pramanik1, Arne Kutzner, Klaus Heese
1Graduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul, 133-791, Republic of Korea.
Abstract:
FAM72A (p17) is a novel neuronal protein that has been linked to tumorigenic effects in non-neuronal tissue. Using state of the art in silico physicochemical analyses (e.g., I-TASSER, RaptorX, and Modeller), we determined the three-dimensional (3D) protein structure of FAM72A and further identified potential ligand-protein interactions. Our data indicate a Zn(2+)/Fe(3+)-containing 3D protein structure, based on a 3GA3_A model template, which potentially interacts with the organic molecule RSM ((2s)-2-(acetylamino)-N-methyl-4-[(R)-methylsulfinyl] butanamide). The discovery of RSM may serve as potential lead for further anti-FAM72A drug screening tests in the pharmaceutical industry because interference with FAM72A's activities via RSM-related molecules might be a novel option to influence the tumor suppressor protein p53 signaling pathways for the treatment of various types of cancers.
Insights
Researchers determined the 3D structure of the novel neuronal protein FAM72A, revealing a potential interaction with the molecule RSM. This finding may lead to new cancer drug screening targeting p53 signaling pathways.
Area of Science:
- Biochemistry
- Structural Biology
- Oncology
Background:
- FAM72A (p17) is a novel neuronal protein implicated in tumorigenesis in non-neuronal tissues.
- Understanding FAM72A's structure and interactions is crucial for developing targeted cancer therapies.
Purpose of the Study:
- To determine the three-dimensional (3D) structure of the FAM72A protein.
- To identify potential ligand-protein interactions involving FAM72A.
- To explore novel therapeutic strategies for cancer treatment by targeting FAM72A.
Main Methods:
- In silico physicochemical analyses using I-TASSER, RaptorX, and Modeller.
- 3D protein structure determination of FAM72A.
- Identification of potential small molecule interactions.
Main Results:
- The 3D structure of FAM72A was elucidated, revealing a Zn(2+)/Fe(3+)-containing structure.
- A potential interaction between FAM72A and the organic molecule RSM ((2s)-2-(acetylamino)-N-methyl-4-[(R)-methylsulfinyl] butanamide) was identified.
- RSM may serve as a lead compound for drug screening.
Conclusions:
- The structural insights into FAM72A and its interaction with RSM offer a novel avenue for cancer drug development.
- Targeting FAM72A activity through RSM-related molecules could influence tumor suppressor protein p53 signaling.
- This research opens possibilities for new therapeutic strategies in various cancer types.
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