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

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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.
Publisher
한국구조생물학회
Issue Date
2020-09
Language
English
Citation

Biodesign, v.8, no.3, pp.60 - 63

ISSN
2288-6982
DOI
10.34184/kssb.2020.8.3.60
URI
http://hdl.handle.net/10203/285615
Appears in Collection
MSE-Journal Papers(저널논문)
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