1N99
CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN
1N99 の概要
| エントリーDOI | 10.2210/pdb1n99/pdb |
| 分子名称 | Syntenin 1 (2 entities in total) |
| 機能のキーワード | pdz domain, signaling protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cell junction, focal adhesion: O00560 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 36412.54 |
| 構造登録者 | Kang, B.S.,Cooper, D.R.,Jelen, F.,Devedjiev, Y.,Derewenda, U.,Dauter, Z.,Otlewski, J.,Derewenda, Z.S. (登録日: 2002-11-22, 公開日: 2003-04-15, 最終更新日: 2024-11-06) |
| 主引用文献 | Kang, B.S.,Cooper, D.R.,Jelen, F.,Devedjiev, Y.,Derewenda, U.,Dauter, Z.,Otlewski, J.,Derewenda, Z.S. PDZ Tandem of Human Syntenin: Crystal Structure and Functional Properties Structure, 11:459-468, 2003 Cited by PubMed Abstract: Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin. PubMed: 12679023DOI: 10.1016/S0969-2126(03)00052-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.94 Å) |
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