6MZN

Zebrafish betaglycan orphan domain structure from tetragonal crystal form

6MZN の概要

• エントリーDOI: 10.2210/pdb6mzn/pdb
• 分子名称: Transforming growth factor beta receptor III (2 entities in total)
• 機能のキーワード: proteoglycan, cytokine receptor, co-receptor, protein binding
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37819.18

構造登録者

Hinck, A.P.,Kim, S. (登録日: 2018-11-05, 公開日: 2019-08-21, 最終更新日: 2023-10-11)

主引用文献

Kim, S.K.,Whitley, M.J.,Krzysiak, T.C.,Hinck, C.S.,Taylor, A.B.,Zwieb, C.,Byeon, C.H.,Zhou, X.,Mendoza, V.,Lopez-Casillas, F.,Furey, W.,Hinck, A.P.
Structural Adaptation in Its Orphan Domain Engenders Betaglycan with an Alternate Mode of Growth Factor Binding Relative to Endoglin.
Structure, 27:1427-1442.e4, 2019

PubMed Abstract: Betaglycan (BG) and endoglin (ENG), homologous co-receptors of the TGF-β family, potentiate the signaling activity of TGF-β2 and inhibin A, and BMP-9 and BMP-10, respectively. BG exists as monomer and forms 1:1 growth factor (GF) complexes, while ENG exists as a dimer and forms 2:1 GF complexes. Herein, the structure of the BG orphan domain (BG) reveals an insertion that blocks the region that the endoglin orphan domain (ENG) uses to bind BMP-9, preventing it from binding in the same manner. Using binding studies with domain-deleted forms of TGF-β and BG, as well as small-angle X-ray scattering data, BG is shown to bind its cognate GF in an entirely different manner compared with ENG. The alternative interfaces likely engender BG and ENG with the ability to selectively bind and target their cognate GFs in a unique temporal-spatial manner, without interfering with one another or other TGF-β family GFs.

PubMed: 31327662
DOI: 10.1016/j.str.2019.06.010

実験手法

X-RAY DIFFRACTION (2.38 Å)