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5DRN

Context-independent anti-hypusine antibody FabHpu24 in complex with hypusine

5DRN の概要
エントリーDOI10.2210/pdb5drn/pdb
関連するPDBエントリー5DS8 5DSC 5DTF 5DUB
分子名称Fab Hpu24 Heavy chain, Fab Hpu24 Light chain, Hypusine, ... (5 entities in total)
機能のキーワードhypusine, antibody, fabhpu24, eif5a, immune system
由来する生物種Oryctolagus cuniculus
詳細
タンパク質・核酸の鎖数4
化学式量合計91874.32
構造登録者
Zhai, Q.,Carter, P.J. (登録日: 2015-09-16, 公開日: 2016-01-20, 最終更新日: 2023-11-15)
主引用文献Zhai, Q.,He, M.,Song, A.,Deshayes, K.,Dixit, V.M.,Carter, P.J.
Structural Analysis and Optimization of Context-Independent Anti-Hypusine Antibodies.
J.Mol.Biol., 428:603-617, 2016
Cited by
PubMed Abstract: Context-independent anti-hypusine antibodies that bind to the post-translational modification (PTM), hypusine, with minimal dependence on flanking amino acid sequences, were identified. The antibodies bind to both hypusine and deoxyhypusine or selectively to hypusine but not to deoxyhypusine. Phage display was used to further enhance the affinity of the antibodies. Affinity maturation of these anti-hypusine antibodies improved their performance in affinity capture of the only currently known hypusinated protein, eukaryotic translation initiation factor 5A. These anti-hypusine antibodies may have utility in the identification of novel hypusinated proteins. Crystal structures of the corresponding Fab fragments were determined in complex with hypusine- or deoxyhypusine-containing peptides. The hypusine or deoxyhypusine moiety was found to reside in a deep pocket formed between VH and VL domains of the Fab fragments. Interaction between the antibodies and hypusine includes an extensive hydrogen bond network. These are, to our knowledge, the first reported structures of context-independent anti-PTM antibodies in complex with the corresponding PTM.
PubMed: 26778617
DOI: 10.1016/j.jmb.2016.01.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.994 Å)
構造検証レポート
Validation report summary of 5drn
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2024-10-30に公開中

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