1YXW

A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin

1YXW の概要

• エントリーDOI: 10.2210/pdb1yxw/pdb
• 関連するPDBエントリー: 1AF9
• 分子名称: Tetanus toxin (Tentoxylysin), TYROSINE, GLUTAMIC ACID, ... (5 entities in total)
• 機能のキーワード: tetanus toxin, gd3, ganglioside, beta-trefoil, inhibitors, hydrolase
• 由来する生物種: Clostridium tetani
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51009.46

構造登録者

Jayaraman, S.,Eswaramoorthy, S.,Kumaran, D.,Swaminathan, S. (登録日: 2005-02-22, 公開日: 2005-03-15, 最終更新日: 2023-08-23)

主引用文献

Jayaraman, S.,Eswaramoorthy, S.,Kumaran, D.,Swaminathan, S.
Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin
Proteins, 61:288-295, 2005

PubMed Abstract: Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus (TeNT), which share significant structural and functional similarity. Crystal structures of the binding domain of TeNT complexed with disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a shallow cleft region on the surface of the molecule in the beta-trefoil domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus toxin provides a putative site that could be occupied either by a ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW and DiSia show that YEW competes with DiSia, suggesting that YEW can be used to block ganglioside binding. A comparison with the TeNT binding domain in complex with small molecules, BoNT/A and /B, provides insight into the different modes of ganglioside binding.

PubMed: 16104015
DOI: 10.1002/prot.20595

実験手法

X-RAY DIFFRACTION (2.2 Å)