Original title: Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75
Authors: Štouračová, Renata ; Závada, Jan ; Závadová, Zuzana ; Pastoreková, S. ; Brynda, Jiří ; Fábry, Milan ; Král, Vlastimil ; Hořejší, Magdalena ; Sedláček, Juraj
Document type: Papers
Conference/Event: Meeting of the Czech and Slovak Structural Biologists /2./, Nové Hrady (CZ), 2003-03-13 / 2003-03-15
Year: 2003
Language: eng
Abstract: Carbonic anhydrase IX (CA IX) is a cell surface protein, strongly associated with certain types of human carcinomas. Structural study of a CA IX-binding monoclonal antibody (mAb) M75, complexed with its epitope peptide may contribute toward elucidation of the role of CA IX. Monoclonal antibody M75 was obtained and proved to react excellently with native and denaturated CA IX. Using synthetic oligopeptides, the epitope of mAb M75 was localized in the proteoglycan domain of CA IX, in the region of a tandem repeat and identified as amino acids PGEEDLP. The Fab fragment was obtained by papain cleavage. We obtained crystals of free Fab M75 and Fab M75 complexed with two different epitope peptides. The data set for Fab M75 was collected and the structure solving is underway.
Keywords: anti-carbonic ahydrase antibody, cancer, crystallization
Project no.: CEZ:AV0Z5052915 (CEP)
Host item entry: Material Structure in Chemistry, Biology, Physics and Technology, ISSN 1211-5894

Institution: Institute of Molecular Genetics AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0087283

Permalink: http://www.nusl.cz/ntk/nusl-28134


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