3DMK
Crystal structure of Down Syndrome Cell Adhesion Molecule (DSCAM) isoform 1.30.30, N-terminal eight Ig domains
3DMK の概要
| エントリーDOI | 10.2210/pdb3dmk/pdb |
| 関連するPDBエントリー | 2V5M 2V5R 2V5S |
| 関連するBIRD辞書のPRD_ID | PRD_900017 |
| 分子名称 | Down Syndrome Cell Adhesion Molecule (DSCAM) isoform 1.30.30, N-terminal eight Ig domains, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| 機能のキーワード | ig domains, immunoglobulin domain, cell adhesion |
| 由来する生物種 | Drosophila melanogaster |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 273861.58 |
| 構造登録者 | Sawaya, M.R.,Wojtowicz, W.M.,Eisenberg, D.,Zipursky, S.L. (登録日: 2008-07-01, 公開日: 2008-10-07, 最終更新日: 2024-11-20) |
| 主引用文献 | Sawaya, M.R.,Wojtowicz, W.M.,Andre, I.,Qian, B.,Wu, W.,Baker, D.,Eisenberg, D.,Zipursky, S.L. A double S shape provides the structural basis for the extraordinary binding specificity of Dscam isoforms. Cell(Cambridge,Mass.), 134:1007-1018, 2008 Cited by PubMed Abstract: Drosophila Dscam encodes a vast family of immunoglobulin (Ig)-containing proteins that exhibit isoform-specific homophilic binding. This diversity is essential for cell recognition events required for wiring the brain. Each isoform binds to itself but rarely to other isoforms. Specificity is determined by "matching" of three variable Ig domains within an approximately 220 kD ectodomain. Here, we present the structure of the homophilic binding region of Dscam, comprising the eight N-terminal Ig domains (Dscam(1-8)). Dscam(1-8) forms a symmetric homodimer of S-shaped molecules. This conformation, comprising two reverse turns, allows each pair of the three variable domains to "match" in an antiparallel fashion. Structural, genetic, and biochemical studies demonstrate that, in addition to variable domain "matching," intramolecular interactions between constant domains promote homophilic binding. These studies provide insight into how "matching" at all three pairs of variable domains in Dscam mediates isoform-specific recognition. PubMed: 18805093DOI: 10.1016/j.cell.2008.07.042 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (4.19 Å) |
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