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identifier: 1811893
description:
epitope description:H: Q198, K199, G200, W201, N202, W207, V217, S219, H232, D234, N236, P237, N238, S240, T242, W244; I: A225, R256
antigen name:Lactococcus virus P2 protein
host organism:Lama glama
antibody name:VHH5
aggregation:
instance of dataset
availability:
available
primaryPublications: 20351260
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1020740
landingPage: http://www.iedb.org/assay/1811893
type:
Literature
publicationVenue:
Proc Natl Acad Sci U S A
dates:
2010
study type: b cell assays
subject species: Lactococcus virus P2
fullName:
Giuliano Sciara
Cecilia Bebeacua
Patrick Bron
Denise Tremblay
Miguel Ortiz-Lombardia
Julie Lichiè
re
Marin van Heel
Valé
rie Campanacci
Sylvain Moineau
Christian Cambillau
method:
x-ray crystallography
name:
Structure of lactococcal phage p2 baseplate and its mechanism of activation.
description:
Epitope residues were calculated from [PDB: 2WZP] as recognized by VHH5 (PDB chain ID: J) at 4Å
atomic distance. The antigen trimer is recognized by 3 VHH5s, with each identical epitope located on 2 monomers (Chain H and I) of the trimer.
The structure of cameloid VHH5 bound to RBP/ORF15/ORF16 ensemble was solved by molecular replacement. The structure displays a quasi hexagonal symmetry, and from bottom to top is formed of three ORF16, six ORF15, and six trimers of ORF18 (RBP), as well as 18 VHH5. Strict hexameric symmetry is not observed because ORF16 is trimeric. Furthermore, the symmetry of ORF16 disturbs the hexameric assemblies of ORF15 and ORF18. Each ORF18 trimer is coordinated by three VHH5s, specifically the trimer consisting of PDB chains G, H, I is coordinated by VHH5s chains J, K, and L. Each VHH interacts with 2 monomers of the trimer in similar fashion, thus that all three epitopes are identical (based on calculation).

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