Crystal structure at 1.95 A resolution of the breast tumour-specific antibody SM3 complexed with its peptide epitope reveals novel hypervariable loop recognition.

Title:

Crystal structure at 1.95 A resolution of the breast tumour-specific antibody SM3 complexed with its peptide epitope reveals novel hypervariable loop recognition.

Dataset

identifier:	2019482
description:	epitope description:SAPDTRPAP antigen name:Mucin-1 host organism:Mus musculus BALB/c antibody name:anti-breast tumour antibody SM3
aggregation:	instance of dataset
availability:	available
primaryPublications:	9826510

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1009154
landingPage:	http://www.iedb.org/assay/2019482

Publication

type:	Literature
publicationVenue:	J Mol Biol
dates:	1998

Dimension

study type:	b cell assays
subject species:	Homo sapiens

Person

fullName:	P Dokurno P A Bates H A Band L M Stewart J M Lally J M Burchell J Taylor-Papadimitriou D Snary M J Sternberg P S Freemont

Data Type

method:	antigen inhibition (~ IC50)

Study

name:	Crystal structure at 1.95 A resolution of the breast tumour-specific antibody SM3 complexed with its peptide epitope reveals novel hypervariable loop recognition.
description:	The epitope lies in the repeating unit of the protein MUC1 with approximately 42 repetitions of the sequence PAPGSTAPPAHGVTSAPDTR. Previously, the minimal core of the epitope was shown to be PDTRP. The 13 residue MUC1 peptide competed the binding of epitope-specific SM3 Fab to a recombinant fusion protein containing seven non-glycosylated MUC1 repeats. The MUC1 peptide bound SM3 with an apparent Ka of 24 µM.

Data Repository

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

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