Crystallization and preliminary diffraction analysis of Bak incubated with eltrombopag

• 영문명: Crystallization and preliminary diffraction analysis of Bak incubated with eltrombopag
• 발행기관: 한국구조생물학회
• 저자명: Dahwan Lim So Hyeon Park Ho-Chul Shin Seung Jun Kim Bonsu Ku
• 간행물 정보: 『Biodesign』Vol 12, No 1, Mar, 8~12쪽, 전체 5쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2024.03.30

영문 초록

Bak is the proapoptotic Bcl-2 protein family member, forming an oligomerized pore at the mitochondrial outer membrane for the release of cytochrome c from the mitochondria into the cytosol. Due to its apoptosis-triggering role, Bak is considered a potential therapeutic drug target. Notably, eltrombopag, an FDA-approved thrombopoietin receptor agonist, was identified as a novel Bak-binding proapoptotic molecule. In this study, the recombinant Bak protein produced in Escherichia coli was purified and then mixed with eltrombopag at a 1:1.2 molar ratio. Crystals were obtained using the sample, and utilized to collect X-ray diffraction data with a maximum resolution of 1.40 Å. Preliminary diffraction analysis indicated that our crystals belonged to the P63 space group with unit cell parameters a = b = 73.5 Å and c = 44.6 Å. In a single asymmetric unit, one protein molecule is present, with a 36.5% solvent content and a 1.94 Å3/Da Matthews coefficient.

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INTRODUCTION

RESULTS AND DISCUSSION

METHODS

ACKNOWLEDGEMENTS

CONFLICT OF INTEREST

REFERENCES