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identifier: 1846597
description:
epitope description:T68, I127, R131, I135, T136, P138, F139, V222, A226, K267, E268, A271, T274, L275, I278, I325, Y326, R328, P330
antigen name:Beta-2 adrenergic receptor
host organism:Lama glama
antibody name:Nb80
aggregation:
instance of dataset
availability:
available
primaryPublications: 21228869
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1022177
landingPage: http://www.iedb.org/assay/1846597
type:
Literature
publicationVenue:
Nature
dates:
2011
study type: b cell assays
subject species: Homo sapiens
fullName:
ren G F Rasmussen
Hee-Jung Choi
Juan Jose Fung
Els Pardon
Paola Casarosa
Pil Seok Chae
Brian T Devree
Daniel M Rosenbaum
Foon Sun Thian
Tong Sun Kobilka
Andreas Schnapp
Ingo Konetzki
Roger K Sunahara
Samuel H Gellman
Alexander Pautsch
Jan Steyaert
William I Weis
Brian K Kobilka
method:
biological activity
name:
Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor.
description:
The epitope residues are calculated from the PDB structure [PDB: 3P0G] as the antigen residues at 4 Å
distance from the antibody.
Binding of epitope-specific nanobody Nb80 to the ß2AR-T4 lysozyme fusion protein, reconstituted into HDL particles, increased the affinity of the agonist isoproterenol for ß2AR-T4L, similar to the increase observed in the Gs-coupled state. Nb80 did not affect ß2AR-T4L binding to the inverse agonist ICI-118551. In the fusion protein, the third intracellular loop of ß2AR was replaced by T4 lysozyme.

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