5TLK

COMPLEX BETWEEN HUMAN CD27 AND FAB FRAGMENTS OF ANTIBODIES M2177 AND H2191

5TLK の概要

• エントリーDOI: 10.2210/pdb5tlk/pdb
• 関連するPDBエントリー: 5TL5 5TLJ
• 分子名称: M2177 LIGHT CHAIN, M2177 HEAVY CHAIN, H2191 LIGHT CHAIN, ... (7 entities in total)
• 機能のキーワード: immune system
• 由来する生物種: Mus musculus, Homo sapiens (Mouse, Human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P26842
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 218117.00

構造登録者

Teplyakov, A.,Obmolova, G.,Malia, T.,Gilliland, G.L. (登録日: 2016-10-11, 公開日: 2017-02-08, 最終更新日: 2024-10-23)

主引用文献

Obmolova, G.,Teplyakov, A.,Malia, T.J.,Wunderler, N.,Kwok, D.,Barone, L.,Sweet, R.,Ort, T.,Scully, M.,Gilliland, G.L.
Epitope-dependent mechanisms of CD27 neutralization revealed by X-ray crystallography.
Mol. Immunol., 83:92-99, 2017

PubMed Abstract: CD27 is a T and B cell co-stimulatory protein of the TNF receptor superfamily dependent on the availability of the TNF-like ligand CD70. Two anti-CD27 neutralizing monoclonal antibodies were obtained from mouse hybridoma and subsequently humanized and optimized for binding the target. The two antibodies are similar in terms of their CD27-binding affinity and ability to block NF-κB signaling, however their clearance rates in monkeys are very different. The pharmacokinetics profiles could be epitope dependent. To identify the epitopes, we determined the crystal structure of the ternary complex between CD27 and the Fab fragments of these non-competing antibodies. The structure reveals the binding modes of the antibodies suggesting that their mechanisms of action are distinctly different and provides a possible explanation of the in vivo data.

PubMed: 28119207
DOI: 10.1016/j.molimm.2017.01.005

実験手法

X-RAY DIFFRACTION (2.7 Å)