5Y7D

Crystal structure of human Endothelial-overexpressed LPS associated factor 1

5Y7D の概要

• エントリーDOI: 10.2210/pdb5y7d/pdb
• 分子名称: Protein CXorf40A, GLYCEROL, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: endothelial-overexpressed lps associated factor 1, rna binding domain, pua domain, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18861.28

構造登録者

Park, S.H.,Kim, M.J.,Park, J.S.,Kim, H.J.,Han, B.W. (登録日: 2017-08-17, 公開日: 2018-08-22, 最終更新日: 2024-03-27)

主引用文献

Kim, M.,Park, S.H.,Park, J.S.,Kim, H.J.,Han, B.W.
Crystal Structure of Human EOLA1 Implies Its Possibility of RNA Binding.
Molecules, 24:-, 2019

PubMed Abstract: Human endothelial-overexpressed lipopolysaccharide-associated factor 1 (EOLA1) has been suggested to regulate inflammatory responses in endothelial cells by controlling expression of proteins, interleukin-6 and vascular cell adhesion molecule-1, and by preventing apoptosis. To elucidate the structural basis of the EOLA1 function, we determined its crystal structure at 1.71 Å resolution and found that EOLA1 is structurally similar to an activating signal cointegrator-1 homology (ASCH) domain with a characteristic β-barrel fold surrounded by α-helices. Despite its low sequence identity with other ASCH domains, EOLA1 retains a conserved 'xxxx' motif in its cavity structure. The cavity harbors aromatic and polar residues, which are speculated to accommodate nucleotide molecules as do YT521-B homology (YTH) proteins. Additionally, EOLA1 exhibits a positively charged cleft, similar to those observed in YTH proteins and the ASCH protein from that exerts ribonuclease activity. This implies that the positively charged cleft in EOLA1 could stabilize the binding of RNA molecules. Taken together, we suggest that EOLA1 controls protein expression through RNA binding to play protective roles against endothelial cell injuries resulting from lipopolysaccharide (LPS)-induced inflammation responses.

PubMed: 31569543
DOI: 10.3390/molecules24193529

実験手法

X-RAY DIFFRACTION (1.71 Å)