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Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75
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SYSNO ASEP 0191539 Document Type K - Proceedings Paper (Czech conf.) R&D Document Type Conference Paper Title Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75 Author(s) Štouračová, Renata (UMG-J)
Závada, Jan (UMG-J)
Závadová, Zuzana (UMG-J)
Pastoreková, S. (SK)
Brynda, Jiří (UMG-J) RID
Fábry, Milan (UMG-J) RID
Král, Vlastimil (UMG-J) RID
Hořejší, Magdalena (UMG-J)
Sedláček, Juraj (UMG-J) RIDSource Title Material Structure in Chemistry, Biology, Physics and Technology. - Praha, Česká republika : Czech and Slovak Crystallographic Association, 2003 - ISSN 1211-5894
s. 70Number of pages 1 s. Action Meeting of the Czech and Slovak Structural Biologists /2./ Event date 13.03.2003-15.03.2003 VEvent location Nové Hrady Country CZ - Czech Republic Event type EUR Language eng - English Country CZ - Czech Republic Keywords anti-carbonic ahydrase antibody, cancer, crystallization Subject RIV BO - Biophysics CEZ AV0Z5052915 - UMG-J Annotation 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. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2004
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