Human leucine-rich-alpha-2-glycoprotein1: purification, crystallization, and X-ray crystallographic analysis

• 발행기관: 한국구조생물학회
• 저자명: Beom Seok Park Seoung Youn Won Dong Sun Lee Ho Min Kim
• 간행물 정보: 『Biodesign』Vol 8, No 3, Sep, 60~63쪽, 전체 4쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2020.09.30

영문 초록

Leucine-rich-alpha-2-glycoprotein1 (LRG1), a serum protein produced by hepatocytes, functions as a modulator of transforming growth factor beta1 (TGFβ1) signaling in angiogenesis and tumor progression. However, structural studies of LRG1 and detailed binding partner’s interactions have not been reported. To understand structural features and functions of LRG1, purification and crystallization of full length LRG1 were performed in the present study. The crystal of LRG1 diffracted X-rays at a resolution of 2.5 Å. The crystal belonged to space group P6322, having unit cell parameters of a = 143.02 Å, b = 143.02 Å, c = 113.73 Å, α = β = 90º, and γ = 120º with five LRG1 molecules present in the asymmetric unit.

목차

INTRODUCTION

RESULTS AND DISCUSSION

MATERIALS AND METHODS

REFERENCES