1RJ7

Crystal structure of EDA-A1

Summary for 1RJ7

• Entry DOI: 10.2210/pdb1rj7/pdb
• Related: 1RJ8
• Descriptor: Ectodysplasin A (2 entities in total)
• Functional Keywords: eda, tnf, beta-bulge, morphogen, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Single-pass type II membrane protein . Ectodysplasin-A, secreted form: Secreted : Q92838
• Total number of polymer chains: 12
• Total formula weight: 214611.52

Authors

Hymowitz, S.G.,Compaan, D.M.,Yan, M.,Ackerly, H.,Dixit, V.M.,Starovasnik, M.A.,de Vos, A.M. (deposition date: 2003-11-18, release date: 2003-12-09, Last modification date: 2023-08-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)