7B01

ADAMTS13-CUB12

7B01 の概要

• エントリーDOI: 10.2210/pdb7b01/pdb
• 分子名称: Maltodextrin-binding protein,Maltodextrin-binding protein,Maltodextrin-binding protein,ADAMTS13 CUB12,A disintegrin and metalloproteinase with thrombospondin motifs 13,A disintegrin and metalloproteinase with thrombospondin motifs 13,A disintegrin and metalloproteinase with thrombospondin motifs 13, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: adamts13, cub, metalloprotease, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67309.03

構造登録者

Kim, H.J.,Emsley, J. (登録日: 2020-11-18, 公開日: 2021-04-28, 最終更新日: 2024-11-06)

主引用文献

Kim, H.J.,Xu, Y.,Petri, A.,Vanhoorelbeke, K.,Crawley, J.T.B.,Emsley, J.
Crystal structure of ADAMTS13 CUB domains reveals their role in global latency.
Sci Adv, 7:-, 2021

PubMed Abstract: ADAMTS13 is a plasma metalloprotease that is essential for the regulation of von Willebrand factor (VWF) function, mediator of platelet recruitment to sites of blood vessel damage. ADAMTS13 function is dynamically regulated by structural changes induced by VWF binding that convert it from a latent to active conformation. ADAMTS13 global latency is manifest by the interaction of its C-terminal CUB1-2 domains with its central Spacer domain. We resolved the crystal structure of the ADAMTS13 CUB1-2 domains revealing a previously unreported configuration for the tandem CUB domains. Docking simulations between the CUB1-2 domains with the Spacer domain in combination with enzyme kinetic functional characterization of ADAMTS13 CUB domain mutants enabled the mapping of the CUB1-2 domain site that binds the Spacer domain. Together, these data reveal the molecular basis of the ADAMTS13 Spacer-CUB interaction and the control of ADAMTS13 global latency.

PubMed: 33863735
DOI: 10.1126/sciadv.abg4403

実験手法

X-RAY DIFFRACTION (2.8 Å)