5LQ2

Crystal structure of Tyr24 phosphorylated Annexin A2 at 3.4 A resolution

5LQ2 の概要

• エントリーDOI: 10.2210/pdb5lq2/pdb
• 関連するPDBエントリー: 5LPU
• 分子名称: Annexin A2, CALCIUM ION (3 entities in total)
• 機能のキーワード: calcium-binding protein, tyrosine phosphorylation
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix, basement membrane : P07355
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77788.62

構造登録者

Ecsedi, P.,Gogl, G.,Kiss, B.,Nyitray, L. (登録日: 2016-08-15, 公開日: 2017-07-05, 最終更新日: 2024-11-13)

主引用文献

Ecsedi, P.,Kiss, B.,Gogl, G.,Radnai, L.,Buday, L.,Koprivanacz, K.,Liliom, K.,Leveles, I.,Vertessy, B.,Jeszenoi, N.,Hetenyi, C.,Schlosser, G.,Katona, G.,Nyitray, L.
Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding.
Structure, 25:1195-1207.e5, 2017

PubMed Abstract: Annexin A2 (ANXA2) has a versatile role in membrane-associated functions including membrane aggregation, endo- and exocytosis, and it is regulated by post-translational modifications and protein-protein interactions through the unstructured N-terminal domain (NTD). Our sequence analysis revealed a short motif responsible for clamping the NTD to the C-terminal core domain (CTD). Structural studies indicated that the flexibility of the NTD and CTD are interrelated and oppositely regulated by Tyr24 phosphorylation and Ser26Glu phosphomimicking mutation. The crystal structure of the ANXA2-S100A4 complex showed that asymmetric binding of S100A4 induces dislocation of the NTD from the CTD and, similar to the Ser26Glu mutation, unmasks the concave side of ANXA2. In contrast, pTyr24 anchors the NTD to the CTD and hampers the membrane-bridging function. This inhibition can be restored by S100A4 and S100A10 binding. Based on our results we provide a structural model for regulation of ANXA2-mediated membrane aggregation by NTD phosphorylation and S100 binding.

PubMed: 28669632
DOI: 10.1016/j.str.2017.06.001

実験手法

X-RAY DIFFRACTION (3.4 Å)