4LGR

Ricin A chain bound to camelid nanobody (VHH3)

4LGR の概要

• エントリーDOI: 10.2210/pdb4lgr/pdb
• 関連するPDBエントリー: 4LGP 4LGS 4LHJ 4LHQ
• 分子名称: Ricin, Camelid nanobody (VHH3), ZINC ION, ... (7 entities in total)
• 機能のキーワード: ribosome inhibiting protein 2, hydrolase-immune system complex, hydrolase/immune system
• 由来する生物種: Ricinus communis (Castor bean); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42400.67

構造登録者

Rudolph, M.J.,Cheung, J.,Franklin, M.,Burshteyn, F.,Cassidy, M.,Gary, E.,Mantis, N. (登録日: 2013-06-28, 公開日: 2014-06-11, 最終更新日: 2024-10-30)

主引用文献

Rudolph, M.J.,Vance, D.J.,Cheung, J.,Franklin, M.C.,Burshteyn, F.,Cassidy, M.S.,Gary, E.N.,Herrera, C.,Shoemaker, C.B.,Mantis, N.J.
Crystal Structures of Ricin Toxin's Enzymatic Subunit (RTA) in Complex with Neutralizing and Non-Neutralizing Single-Chain Antibodies.
J.Mol.Biol., 426:3057-3068, 2014

PubMed Abstract: Ricin is a select agent toxin and a member of the RNA N-glycosidase family of medically important plant and bacterial ribosome-inactivating proteins. In this study, we determined X-ray crystal structures of the enzymatic subunit of ricin (RTA) in complex with the antigen binding domains (VHH) of five unique single-chain monoclonal antibodies that differ in their respective toxin-neutralizing activities. None of the VHHs made direct contact with residues involved in RTA's RNA N-glycosidase activity or induced notable allosteric changes in the toxin's subunit. Rather, the five VHHs had overlapping structural epitopes on the surface of the toxin and differed in the degree to which they made contact with prominent structural elements in two folding domains of the RTA. In general, RTA interactions were influenced most by the VHH CDR3 (CDR, complementarity-determining region) elements, with the most potent neutralizing antibody having the shortest and most conformationally constrained CDR3. These structures provide unique insights into the mechanisms underlying toxin neutralization and provide critically important information required for the rational design of ricin toxin subunit vaccines.

PubMed: 24907552
DOI: 10.1016/j.jmb.2014.05.026

実験手法

X-RAY DIFFRACTION (1.65 Å)