5AEA
Crystal structure of human NCAM domain 1
5AEA の概要
| エントリーDOI | 10.2210/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 | |
| 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: 27036939DOI: 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) |
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