Název:
Crystallographic study of an anti=carbonic anhydrase IX monoclonal antibody M75
Autoři:
Štouračová, Renata ; Závada, Jan ; Závadová, Zuzana ; Pastoreková, S. ; Brynda, Jiří ; Fábry, Milan ; Král, Vlastimil ; Hořejší, Magdalena ; Sedláček, Juraj Typ dokumentu: Příspěvky z konference Konference/Akce: Meeting of the Czech and Slovak Structural Biologists /2./, Nové Hrady (CZ), 2003-03-13 / 2003-03-15
Rok:
2003
Jazyk:
eng
Abstrakt: 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.
Klíčová slova:
anti-carbonic ahydrase antibody, cancer, crystallization Číslo projektu: CEZ:AV0Z5052915 (CEP) Zdrojový dokument: Material Structure in Chemistry, Biology, Physics and Technology, ISSN 1211-5894
Instituce: Ústav molekulární genetiky AV ČR
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Informace o dostupnosti dokumentu:
Dokument je dostupný v příslušném ústavu Akademie věd ČR. Původní záznam: http://hdl.handle.net/11104/0087283