3QW9

Crystal structure of betaglycan ZP-C domain

3QW9 の概要

• エントリーDOI: 10.2210/pdb3qw9/pdb
• 分子名称: Transforming growth factor beta receptor type 3, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: cytokine receptor, immunoglobulin domain, zona pellucida, tgf-beta ligand co-receptor, protein polymerization
• 由来する生物種: Rattus norvegicus (rat)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42237.99

構造登録者

Lin, S.J.,Jardetzky, T.S. (登録日: 2011-02-27, 公開日: 2011-04-06, 最終更新日: 2024-12-25)

主引用文献

Lin, S.J.,Hu, Y.,Zhu, J.,Woodruff, T.K.,Jardetzky, T.S.
Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-{beta} binding.
Proc.Natl.Acad.Sci.USA, 108:5232-5236, 2011

PubMed Abstract: The zona pellucida (ZP) domain is a bipartite protein structural element comprised of ZP-N and ZP-C regions. Most notable for its ability to mediate protein polymerization, many ZP proteins polymerize and assemble into long fibrils that form specialized extracellular matrices. Other ZP proteins (namely, betaglycan and endoglin) do not polymerize but serve as important membrane coreceptors for ligands in the transforming growth factor-β (TGF-β) superfamily. Here, we present the 2.0-Å resolution crystal structure of the betaglycan ZP-C region in combination with a downstream region known as the external hydrophobic patch (EHP). Similar to the ZP-N region, the ZP-C region also adopts an immunoglobulin-like fold, despite sharing no sequence homology and possessing different disulfide linkages. The EHP region, which was previously thought to be external to the ZP region, is integral to the ZP-C domain and corresponds to the ZP-C G strand. Our structure also indicates that the critical maturation cleavage of ZP proteins, a process that activates nascent ZP proteins for polymerization, occurs within the immunoglobulin domain at the FG loop. Nonpolymerizing ZP proteins such as betaglycan and endoglin do not contain this cleavage site. Finally, our structure suggests that the AB loop and the convex surface pocket are regions important for TGF-β ligand binding.

PubMed: 21402931
DOI: 10.1073/pnas.1010689108

実験手法

X-RAY DIFFRACTION (2 Å)