1RJ7

Crystal structure of EDA-A1

1RJ7 の概要

• エントリーDOI: 10.2210/pdb1rj7/pdb
• 関連するPDBエントリー: 1RJ8
• 分子名称: Ectodysplasin A (2 entities in total)
• 機能のキーワード: eda, tnf, beta-bulge, morphogen, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane ; Single-pass type II membrane protein . Ectodysplasin-A, secreted form: Secreted : Q92838
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 214611.52

構造登録者

Hymowitz, S.G.,Compaan, D.M.,Yan, M.,Ackerly, H.,Dixit, V.M.,Starovasnik, M.A.,de Vos, A.M. (登録日: 2003-11-18, 公開日: 2003-12-09, 最終更新日: 2023-08-23)

主引用文献

Hymowitz, S.G.,Compaan, D.M.,Yan, M.,Wallweber, H.J.,Dixit, V.M.,Starovasnik, M.A.,de Vos, A.M.
The crystal structures of EDA-A1 and EDA-A2: splice variants with distinct receptor specificity.
Structure, 11:1513-1520, 2003

PubMed Abstract: EDA is a tumor necrosis factor family member involved in ectodermal development. Splice variants EDA-A1 and EDA-A2 differ only by the presence of Glu 308 and Val 309 in the expected receptor binding region of EDA-A1 but not EDA-A2. This two amino acid difference functions as a switch controlling receptor specificity. EDA-A1 binds only to EDAR, while EDA-A2 is specific for XEDAR. In order to understand the structural basis of this switch, we determined the X-ray crystal structures of the TNF domain of both EDA-A1 and EDA-A2 at 2.3 A and 2.2 A, respectively. While the backbone conformation around the splice difference is similar in both isoforms, the conformation of the following loop, the surface charge, and the shape of the expected receptor binding site differ significantly.

PubMed: 14656435
DOI: 10.1016/j.str.2003.11.009

実験手法

X-RAY DIFFRACTION (2.3 Å)