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3N7M

Crystal structure of W1252A mutant of HCR D/C VPI 5995

3N7M の概要
エントリーDOI10.2210/pdb3n7m/pdb
関連するPDBエントリー3N7J 3N7K 3N7L
分子名称Neurotoxin, SULFATE ION, GLYCEROL, ... (4 entities in total)
機能のキーワードbotulinum neurotoxin, w1252a mutant, gm1a, ganglioside binding loop, toxin
由来する生物種Clostridium botulinum
タンパク質・核酸の鎖数1
化学式量合計49111.20
構造登録者
Fu, Z.,Karalewitz, A.,Kroken, A.,Baldwin, M.R.,Barbieri, J.T.,Kim, J.-J.P. (登録日: 2010-05-27, 公開日: 2010-09-08, 最終更新日: 2023-09-06)
主引用文献Karalewitz, A.P.,Kroken, A.R.,Fu, Z.,Baldwin, M.R.,Kim, J.J.,Barbieri, J.T.
Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA .
Biochemistry, 49:8117-8126, 2010
Cited by
PubMed Abstract: The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A-G) based on a lack of cross antiserum neutralization. BoNTs utilize gangliosides as components of the host receptors for binding and entry into neurons. Members of BoNT/C and BoNT/D serotypes include mosaic toxins that are organized in D/C and C/D toxins. One D/C mosaic toxin, BoNT/D-South Africa (BoNT/D-SA), was not fully neutralized by immunization with BoNT serotype C or D, which stimulated this study. Here the crystal structures of the receptor binding domains of BoNT/C, BoNT/D, and BoNT/D-SA are presented. Biochemical and cell binding studies show that BoNT/C and BoNT/D-SA possess unique mechanisms for ganglioside binding. These studies provide new information about how the BoNTs can enter host cells as well as a basis for understanding the immunological diversity of these neurotoxins.
PubMed: 20731382
DOI: 10.1021/bi100865f
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 3n7m
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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