1AD9
IGG-FAB FRAGMENT OF ENGINEERED HUMAN MONOCLONAL ANTIBODY CTM01
1AD9 の概要
エントリーDOI | 10.2210/pdb1ad9/pdb |
分子名称 | IGG CTM01 FAB (LIGHT CHAIN), IGG CTM01 FAB (HEAVY CHAIN), SULFATE ION, ... (4 entities in total) |
機能のキーワード | immunoglobulin, fab fragment |
由来する生物種 | Homo sapiens (human) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 96039.19 |
構造登録者 | |
主引用文献 | Banfield, M.J.,King, D.J.,Mountain, A.,Brady, R.L. VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs. Proteins, 29:161-171, 1997 Cited by PubMed Abstract: The crystal structures of two pairs of Fab fragments have been determined. The pairs comprise both a murine and an engineered human form, each derived from the antitumor antibodies A5B7 and CTM01. Although antigen specificity is maintained within the pairs, antigen affinity varies. A comparison of the hypervariable loops for each pair of antibodies shows their structure has been well maintained in grafting, supporting the canonical loop model. Detailed structural analysis of the binding sites and domain arrangements for these antibodies suggests the differences in antigen affinity observed are likely to be due to inherent flexibility of the hypervariable loops and movements at the VL:VH domain interface. The four structures provide the first opportunity to study in detail the effects of protein engineering on specific antibodies. PubMed: 9329081DOI: 10.1002/(SICI)1097-0134(199710)29:2<161::AID-PROT4>3.0.CO;2-G 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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