pISSN 2288-6982
eISSN 2288-7105




BioDesign 2020; 8(3): 60-63

Published online September 30, 2020

© Korean Society for Structural Biology

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

Beom Seok Park1,2, Seoung Youn Won3, Dong Sun Lee4 and Ho Min Kim3,4,*

1Department of Biomedical Laboratory Science, Eulji University, Seongnam 13135, Republic of Korea
2Department of Senior Healthcare, BK21 Plus Program, Eulji University, Daejeon 34824, Republic of Korea
3Graduate School of Medical Science & Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea
4Center for Biomolecular & Cellular Structure, Institute for Basic Science (IBS), Daejeon 34126, Republic of Korea

Correspondence to:

Received: July 7, 2020; Revised: July 25, 2020; Accepted: July 28, 2020


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.