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5XA5

Crystal structure of HMP-1-HMP-2 complex

5XA5 の概要
エントリーDOI10.2210/pdb5xa5/pdb
分子名称Alpha-catenin-like protein hmp-1, Beta-catenin-like protein hmp-2 (3 entities in total)
機能のキーワードfive-helix bundle, cell adhesion
由来する生物種Caenorhabditis elegans
詳細
タンパク質・核酸の鎖数2
化学式量合計35984.40
構造登録者
Shao, X.,Kang, H.,Weis, W.I.,Hardin, J.,Choi, H.J. (登録日: 2017-03-11, 公開日: 2017-08-30, 最終更新日: 2024-03-27)
主引用文献Shao, X.,Kang, H.,Loveless, T.,Lee, G.R.,Seok, C.,Weis, W.I.,Choi, H.J.,Hardin, J.
Cell-cell adhesion in metazoans relies on evolutionarily conserved features of the alpha-catenin· beta-catenin-binding interface.
J.Biol.Chem., 292:16477-16490, 2017
Cited by
PubMed Abstract: Stable tissue integrity during embryonic development relies on the function of the cadherin·catenin complex (CCC). The CCC is a useful paradigm for analyzing requirements for specific interactions among the core components of the CCC, and it provides a unique opportunity to examine evolutionarily conserved mechanisms that govern the interaction between α- and β-catenin. HMP-1, unlike its mammalian homolog α-catenin, is constitutively monomeric, and its binding affinity for HMP-2/β-catenin is higher than that of α-catenin for β-catenin. A crystal structure shows that the HMP-1·HMP-2 complex forms a five-helical bundle structure distinct from the structure of the mammalian α-catenin·β-catenin complex. Deletion analysis based on the crystal structure shows that the first helix of HMP-1 is necessary for binding HMP-2 avidly and for efficient recruitment of HMP-1 to adherens junctions in embryos. HMP-2 Ser-47 and Tyr-69 flank its binding interface with HMP-1, and we show that phosphomimetic mutations at these two sites decrease binding affinity of HMP-1 to HMP-2 by 40-100-fold experiments using HMP-2 S47E and Y69E mutants showed that they are unable to rescue () mutants, suggesting that phosphorylation of HMP-2 on Ser-47 and Tyr-69 could be important for regulating CCC formation in Our data provide novel insights into how cadherin-dependent cell-cell adhesion is modulated in metazoans by conserved elements as well as features unique to specific organisms.
PubMed: 28842483
DOI: 10.1074/jbc.M117.795567
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 5xa5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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