Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75

0191539 - UMG-J 20033033 RIV CZ eng K - Conference Paper (Czech conference)
Štouračová, Renata - Závada, Jan - Závadová, Zuzana - Pastoreková, S. - Brynda, Jiří - Fábry, Milan - Král, Vlastimil - Hořejší, Magdalena - Sedláček, Juraj
Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75.
Material Structure in Chemistry, Biology, Physics and Technology. Praha, Česká republika: Czech and Slovak Crystallographic Association, 2003, s. 70. ISSN 1211-5894.
[Meeting of the Czech and Slovak Structural Biologists /2./. Nové Hrady (CZ), 13.03.2003-15.03.2003]
Institutional research plan: CEZ:AV0Z5052915
Keywords : anti-carbonic ahydrase antibody, cancer, crystallization
Subject RIV: BO - Biophysics

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.
Permanent Link: http://hdl.handle.net/11104/0087283