3WVT

Structural and biochemical study of equine lentivirus receptor 1

3WVT の概要

• エントリーDOI: 10.2210/pdb3wvt/pdb
• 分子名称: ELR1 (2 entities in total)
• 機能のキーワード: tumor necrosis factor receptor, cysteine rich domain, protein binding
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20722.08

構造登録者

Qian, L. (登録日: 2014-06-07, 公開日: 2015-06-10, 最終更新日: 2024-10-30)

主引用文献

Qian, L.,Han, X.D.,Liu, X.Q.
Structural insight into equine lentivirus receptor 1
Protein Sci., 24:633-642, 2015

PubMed Abstract: Equine lentivirus receptor 1 (ELR1) has been identified as a functional cellular receptor for equine infectious anemia virus (EIAV). Herein, recombinant ELR1 and EIAV surface glycoprotein gp90 were respectively expressed in Drosophila melanogaster S2 cells, and purified to homogeneity by Ni-NTA affinity chromatography and gel filtration chromatography. Gel filtration chromatography and analytical ultracentrifugation (AUC) analyses indicated that both ELR1 and gp90 existed as individual monomers in solution and formed a complex with a stoichiometry of 1:1 when mixed. The structure of ELR1 was first determined with the molecular replacement method, which belongs to the space group P42 21 2 with one molecule in an asymmetric unit. It contains eight antiparallel β-sheets, of which four are in cysteine rich domain 1 (CRD1) and two are in CRD2 and CRD3, respectively. Alignment of ELR1 with HVEM and CD134 indicated that Tyr61, Leu70, and Gly72 in CRD1 of ELR1 are important residues for binding to gp90. Isothermal titration calorimetry (ITC) experiments further confirmed that Leu70 and Gly72 are the critical residues.

PubMed: 25559821
DOI: 10.1002/pro.2634

実験手法

X-RAY DIFFRACTION (1.601 Å)