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5AEA

Crystal structure of human NCAM domain 1

5AEA の概要
エントリーDOI10.2210/pdb5aea/pdb
分子名称NEURAL CELL ADHESION MOLECULE 1, CITRATE ANION (3 entities in total)
機能のキーワードcell adhesion, ncam
由来する生物種HOMO SAPIENS (HUMAN)
タンパク質・核酸の鎖数2
化学式量合計26020.90
構造登録者
Kvansakul, M.,Griffiths, K.,Foley, M. (登録日: 2015-08-27, 公開日: 2016-04-13, 最終更新日: 2024-11-20)
主引用文献Griffiths, K.,Dolezal, O.,Cao, B.,Nilsson, S.K.,See, H.B.,Pfleger, K.D.G.,Roche, M.,Gorry, P.R.,Pow, A.,Viduka, K.,Lim, K.,Lu, B.G.C.,Chang, D.H.C.,Murray-Rust, T.,Kvansakul, M.,Perugini, M.A.,Dogovski, C.,Doerflinger, M.,Zhang, Y.,Parisi, K.,Casey, J.L.,Nuttall, S.D.,Foley, M.
I-Bodies, Human Single Domain Antibodies that Antagonize Chemokine Receptor Cxcr4.
J.Biol.Chem., 291:12641-, 2016
Cited by
PubMed Abstract: CXCR4 is a G protein-coupled receptor with excellent potential as a therapeutic target for a range of clinical conditions, including stem cell mobilization, cancer prognosis and treatment, fibrosis therapy, and HIV infection. We report here the development of a fully human single-domain antibody-like scaffold termed an "i-body," the engineering of which produces an i-body library possessing a long complementarity determining region binding loop, and the isolation and characterization of a panel of i-bodies with activity against human CXCR4. The CXCR4-specific i-bodies show antagonistic activity in a range of in vitro and in vivo assays, including inhibition of HIV infection, cell migration, and leukocyte recruitment but, importantly, not the mobilization of hematopoietic stem cells. Epitope mapping of the three CXCR4 i-bodies AM3-114, AM4-272, and AM3-523 revealed binding deep in the binding pocket of the receptor.
PubMed: 27036939
DOI: 10.1074/JBC.M116.721050
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 5aea
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2026-01-28に公開中

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