A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic alpha-exosite binding region.

Title:

A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic alpha-exosite binding region.

Dataset

identifier:	1774310
description:	epitope description:D102, R105, M106, R113, K340, I348, N353, K356, F357 antigen name:Botulinum neurotoxin type A (UniProt:A5HZZ9) host organism:Lama glama antibody name:Aa1 VHH
aggregation:	instance of dataset
availability:	available
primaryPublications:	20138889

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1019673
landingPage:	http://www.iedb.org/assay/1774310

Publication

type:	Literature
publicationVenue:	J Mol Biol
dates:	2010

Dimension

study type:	b cell assays
subject species:	Clostridium botulinum A str. Hall

Person

fullName:	Jianbo Dong Aaron A Thompson Yongfeng Fan Jianlong Lou Fraser Conrad Mengfei Ho Melissa Pires-Alves Brenda A Wilson Raymond C Stevens James D Marks

Data Type

method:	x-ray crystallography

Study

name:	A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic alpha-exosite binding region.
description:	The epitope residues were calculated from [PDB: 3K3Q] as the antigen residues at 4Å atomic distance from the antibody. The epitope of Aa1 VHH on BoNT/A light chain (Lc 425) was determined from the crystal structure of the complex solved by molecular replacement. The asymmetric unit contains a single BoNT/A Lc endopeptidase bound by the Aa1 VHH fragment in a 1:1 stoichiometry. Chain B is N-terminal fragment of BoNT catalytic domain (residues 3-250) and Chain C is the C-terminal fragment of BoNT catalytic domain (residues 251-425).

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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