5XA5
Crystal structure of HMP-1-HMP-2 complex
5XA5 の概要
| エントリーDOI | 10.2210/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: 28842483DOI: 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) |
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