An ultra-specific avian antibody to phosphorylated tau protein reveals a unique mechanism for phosphoepitope recognition.

Title:

An ultra-specific avian antibody to phosphorylated tau protein reveals a unique mechanism for phosphoepitope recognition.

identifier:	1966733
description:	epitope description:KKVAVVRTPPKSPSSAK + PHOS(T8, S12) antigen name:Microtubule-associated protein tau host organism:Gallus gallus antibody name:anti-pT231/pS235_1
aggregation:	instance of dataset
availability:	available
primaryPublications:	23148212

study type:	b cell assays
subject species:	Homo sapiens

fullName:	Heather H Shih Chao Tu Wei Cao Anne Klein Renee Ramsey Brian J Fennell Matthew Lambert Deirdre Ní Shú illeabhá in Bé né dicte Autin Eugenia Kouranova Sri Laxmanan Steven Braithwaite Leeying Wu Mostafa Ait-Zahra Anthony J Milici Jo Ann Dumin Edward R LaVallie Maya Arai Christopher Corcoran Janet E Paulsen Davinder Gill Orla Cunningham Joel Bard Lydia Mosyak William J J Finlay

method:	x-ray crystallography

name:	An ultra-specific avian antibody to phosphorylated tau protein reveals a unique mechanism for phosphoepitope recognition.
description:	The crystal structure of anti-phospho-tau Fab (pT231/pS235_1) in complex with the epitope was determined. The epitope was synthesized with a C-terminal Cys residue. In the Fab-peptide co-crystal structure, 10 amino acids (225- KVAVVR(pT)PPK-234) are visible, of which six (225KVAVVR(pT231)) interact directly with the Fab fragment. The remaining eight residues of the peptide are disordered.

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

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