Crystallization and preliminary diffraction analysis of the T2I·L262F double mutant form of SHP2

• 영문명: Crystallization and preliminary diffraction analysis of the T2I·L262F double mutant form of SHP2
• 발행기관: 한국구조생물학회
• 저자명: Hye Seon Lee Bonsu Ku Ho-Chul Shin Seung Jun Kim
• 간행물 정보: 『Biodesign』Vol 10, No 4, Dec, 69~72쪽, 전체 4쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2022.12.31

영문 초록

The enzymatic activity of SHP2, whose dysregulation causes malfunctions in diverse cellular signaling, is controlled by the autoinhibitory association between its N-SH2 and phosphatase domains. Various SHP2 genetic mutations, which impair the interaction between the two domains, have been identified to cause RAS-MAPK pathway-associated diseases. In this study, SHP2 containing Noonan syndrome-associated T2I and L262F double mutations was targeted for crystallization. The recombinant protein was prepared using an Escherichia coli expression system, purified using Ni-NTA affinity and size exclusion chromatographies, and then subjected for crystallization. X-ray data diffracted to 3.0 Å resolution were collected and used for preliminary diffraction analysis. The unit cell parameters of the crystals belonging to the P21 space group were a = 45.4 Å, b = 215.0 Å, c = 55.6 Å, and β = 95.7°. The asymmetric unit contains two molecules with a solvent content of 40.7% and a Matthews coefficient of 2.07 Å3/Da.

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INTRODUCTION

RESULTS AND DISCUSSION

METHODS

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