5BMF

Crystal Structure of a Theophylline binding antibody Fab fragment

5BMF の概要

• エントリーDOI: 10.2210/pdb5bmf/pdb
• 分子名称: Fab fragment heavy chain, Fab fragment light chain, 2-(5-{1-[1-(1,3-dimethyl-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl)-4,15-dioxo-8,11-dioxa-5,14-diazaicosan-20-yl]-3,3-dimethyl-6-sulfo-1,3-dihydro-2H-indol-2-ylidene}penta-1,3-dien-1-yl)-1-ethyl-3,3-dimethyl-3H-indolium-5-sulfonate, ... (4 entities in total)
• 機能のキーワード: antibody, hapten binding, theophylline, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49408.18

構造登録者

Bujotzek, A.,Fuchs, A.,Changtao, Q.,Klostermann, S.,Benz, J.,Antes, I.,Dengl, S.,Hoffmann, E.,Georges, G. (登録日: 2015-05-22, 公開日: 2015-07-29, 最終更新日: 2024-11-06)

主引用文献

Bujotzek, A.,Fuchs, A.,Qu, C.,Benz, J.,Klostermann, S.,Antes, I.,Georges, G.
MoFvAb: Modeling the Fv region of antibodies.
Mabs, 7:838-852, 2015

PubMed Abstract: Knowledge of the 3-dimensional structure of the antigen-binding region of antibodies enables numerous useful applications regarding the design and development of antibody-based drugs. We present a knowledge-based antibody structure prediction methodology that incorporates concepts that have arisen from an applied antibody engineering environment. The protocol exploits the rich and continuously growing supply of experimentally derived antibody structures available to predict CDR loop conformations and the packing of heavy and light chain quickly and without user intervention. The homology models are refined by a novel antibody-specific approach to adapt and rearrange sidechains based on their chemical environment. The method achieves very competitive all-atom root mean square deviation values in the order of 1.5 Å on different evaluation datasets consisting of both known and previously unpublished antibody crystal structures.

PubMed: 26176812
DOI: 10.1080/19420862.2015.1068492

実験手法

X-RAY DIFFRACTION (2.8 Å)