Home > Conference materials > Papers > Attempts to differentiate subunits of trimeric and hexameric purine nucleoside phosphorylases by crystal structure and solution studies using purine bases, modified purine nucleosides, acyclonucleosides and their phosphonate analogues
Original title:
Attempts to differentiate subunits of trimeric and hexameric purine nucleoside phosphorylases by crystal structure and solution studies using purine bases, modified purine nucleosides, acyclonucleosides and their phosphonate analogues
Translated title:
Pokusy o rozlišení podjednotek trimerních a hexamerních forem purinnukleosidfosforylázy pomocí krystalové struktury komplexů purinových bází nukleosidů, acyklonukleosidů a jejich fosfonátových analogů
Authors:
Bzowska, A. ; Stepniak, K. ; Olasek, M. ; Dlugosz, M. ; Wielgus-Kutrowska, B. ; Antosiewicz, J. ; Holý, Antonín ; Koellner, G. ; Stroh, A. ; Raszewski, G. ; Steiner, T. ; Frank, J. Document type: Papers Conference/Event: Chemistry of Nucleic Acid Components /13./, Špindlerův Mlýn (CZ), 2005-09-03 / 2005-09-09
Year:
2005
Language:
eng Abstract:
[eng][cze] Attempts to demonstrate and interpret differences between subunits forming biologically active oligomers of low-(calf spleen) and high-molecular mass (E. coli) purine nucleoside phosphorylases (PNP) yielded new crystal structures of both enzymes complexed with ground-state analogue ligands in space groups and with two full trimers and one full hexamer in the asymmetric unit, respectively.Byla studována krystalová struktura trimerní purinnukleosidfosforylázy z telecí sleziny v komplexu s 2,6-diamino-(S)-9-[2-(phosphonomethoxy)propyl]purinem. Mezi subjednotkami nebyly nalezeny žádné rozdíly.
Keywords:
acyclonucleosides; purine bases; purine nucleoside phosphorylases; purinové zásady Project no.: KBN3P04A03524, KBN6P04A00121, KO1477/21, CEZ:AV0Z40550506 (CEP) Funding provider: PSCSR, PSCSR, DFG Host item entry: Chemistry of Nucleic Acid Components, ISBN 80-86241-25-4
Institution: Institute of Organic Chemistry and Biochemistry AS ČR
(web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences. Original record: http://hdl.handle.net/11104/0111818