4BA8
High resolution NMR structure of the C mu3 domain from IgM
4BA8 の概要
| エントリーDOI | 10.2210/pdb4ba8/pdb |
| NMR情報 | BMRB: 18711 |
| 分子名称 | IG MU CHAIN C REGION SECRETED FORM (1 entity in total) |
| 機能のキーワード | immune system, immunoglobulin constant region |
| 由来する生物種 | MUS MUSCULUS |
| 細胞内の位置 | Secreted (Probable): P01872 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11262.79 |
| 構造登録者 | Mueller, R.,Kern, T.,Graewert, M.A.,Madl, T.,Peschek, J.,Groll, M.,Sattler, M.,Buchner, J. (登録日: 2012-09-12, 公開日: 2013-06-12, 最終更新日: 2024-06-19) |
| 主引用文献 | Mueller, R.,Graewert, M.A.,Kern, T.,Madl, T.,Peschek, J.,Sattler, M.,Groll, M.,Buchner, J. High Resolution Structures of the Igm Fc Domains Reveal Principles of its Hexamer Formation Proc.Natl.Acad.Sci.USA, 110:10183-, 2013 Cited by PubMed Abstract: IgM is the first antibody produced during the humoral immune response. Despite its fundamental role in the immune system, IgM is structurally only poorly described. In this work we used X-ray crystallography and NMR spectroscopy to determine the atomic structures of the constant IgM Fc domains (Cµ2, Cµ3, and Cµ4) and to address their roles in IgM oligomerization. Although the isolated domains share the typical Ig fold, they differ substantially in dimerization properties and quaternary contacts. Unexpectedly, the Cµ4 domain and its C-terminal tail piece are responsible and sufficient for the specific polymerization of Cµ4 dimers into covalently linked hexamers of dimers. Based on small angle X-ray scattering data, we present a model of the ring-shaped Cµ4 structure, which reveals the principles of IgM oligomerization. PubMed: 23733956DOI: 10.1073/PNAS.1300547110 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
構造検証レポート
検証レポート(詳細版)
をダウンロード






