5VNV

Crystal structure of Nb.b201

5VNV の概要

• エントリーDOI: 10.2210/pdb5vnv/pdb
• 関連するPDBエントリー: 5VNW
• 分子名称: Nb.b201, PENTAETHYLENE GLYCOL, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: nanobody, synthetic protein, llama, camelid, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14267.01

構造登録者

Kruse, A.C.,McMahon, C. (登録日: 2017-05-01, 公開日: 2018-02-21, 最終更新日: 2024-10-09)

主引用文献

McMahon, C.,Baier, A.S.,Pascolutti, R.,Wegrecki, M.,Zheng, S.,Ong, J.X.,Erlandson, S.C.,Hilger, D.,Rasmussen, S.G.F.,Ring, A.M.,Manglik, A.,Kruse, A.C.
Yeast surface display platform for rapid discovery of conformationally selective nanobodies.
Nat. Struct. Mol. Biol., 25:289-296, 2018

PubMed Abstract: Camelid single-domain antibody fragments ('nanobodies') provide the remarkable specificity of antibodies within a single 15-kDa immunoglobulin V domain. This unique feature has enabled applications ranging from use as biochemical tools to therapeutic agents. Nanobodies have emerged as especially useful tools in protein structural biology, facilitating studies of conformationally dynamic proteins such as G-protein-coupled receptors (GPCRs). Nearly all nanobodies available to date have been obtained by animal immunization, a bottleneck restricting many applications of this technology. To solve this problem, we report a fully in vitro platform for nanobody discovery based on yeast surface display. We provide a blueprint for identifying nanobodies, demonstrate the utility of the library by crystallizing a nanobody with its antigen, and most importantly, we utilize the platform to discover conformationally selective nanobodies to two distinct human GPCRs. To facilitate broad deployment of this platform, the library and associated protocols are freely available for nonprofit research.

PubMed: 29434346
DOI: 10.1038/s41594-018-0028-6

実験手法

X-RAY DIFFRACTION (1.4 Å)