3DIT

Crystal structure of MAD MH2 domain

3DIT の概要

• エントリーDOI: 10.2210/pdb3dit/pdb
• 分子名称: Protein mothers against dpp (2 entities in total)
• 機能のキーワード: mad, tgf-beta, mh2, cytoplasm, developmental protein, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation, signaling protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Cytoplasm: P42003
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 63936.03

構造登録者

Hao, R.,Wu, J.W.,Wang, Z.X. (登録日: 2008-06-20, 公開日: 2009-05-12, 最終更新日: 2023-11-01)

主引用文献

Hao, R.,Chen, L.,Wu, J.W.,Wang, Z.X.
Structure of Drosophila Mad MH2 domain.
Acta Crystallogr.,Sect.F, 64:986-990, 2008

PubMed Abstract: In Drosophila, decapentaplegic (Dpp), a member of the TGF-beta superfamily, plays a pivotal role in control of proliferation, global patterning and induction of specific cell fates. Together with Medea, mother against Dpp (Mad), the founding member of the Smad family, specifically transduces the Dpp signal from the plasma membrane to the nucleus. Here, the crystal structure of the MH2 domain of Mad, which closely matches those of other Smad MH2 domains, is reported at 3.2 A resolution. The conservation of Smad protein structures is consistent with their evolutionary conserved and significant function. Furthermore, sequence alignment revealed that most of the variant amino acids in Smad proteins specific to the BMP pathway (Smad1, Smad5 and Mad) were clustered at the surface. In particular, Ser296 and Asp297 of Mad introduced a negative patch into the positive surface observed in the surface electrostatic potential of Smad1 MH2.

PubMed: 18997322
DOI: 10.1107/S1744309108033034

実験手法

X-RAY DIFFRACTION (3.2 Å)