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Croatica Chemica Acta, Vol.87 No.4 Prosinac 2014.

Izvorni znanstveni članak
DOI: 10.5562/cca2430

Solution Structure of a Prion Protein Aptamer Analogue

Špela Medic ; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
Peter Podbevšek   ORCID icon orcid.org/0000-0002-2563-4507 ; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia;EN-FIST Centre of Excellence, Trg Osvobodilne fronte 13, SI-1000 Ljubljana, Slovenia
Janez Plavec   ORCID icon orcid.org/0000-0003-1570-8602 ; Slovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia;EN-FIST Centre of Excellence, Trg Osvobodilne fronte 13, SI-1000 Ljubljana, Slovenia;Faculty of Chemistry and Chemical Technology, University of Ljubljana, A

Puni tekst: engleski, pdf (1 MB) str. 321-325 preuzimanja: 275* citiraj
APA
Medic, Š., Podbevšek, P., Plavec, J. (2014). Solution Structure of a Prion Protein Aptamer Analogue. Croatica Chemica Acta, 87(4). doi:10.5562/cca2430

Sažetak
It has previously been shown that r(GGA)4 folds into a G-quadruplex structure, which binds to the normal cellular form of the prion protein (PrPC) with high affinity. The current study utilizes CD and NMR spectroscopy to show that a dimeric parallel G-quadruplex structure is formed by r(GGA)2 in a KCl solution. Each r[(GGA)2]2 G-quadruplex unit exhibits two G-quartets, one of which is hydro- gen bonded to two additional adenines forming a hexade. Through stacking of hexade planes, two
G-quadruplex units interact with each other and form a symmetric dimer, r[(GGA)2]4. The topolo¬gy of r[(GGA)2]4 is in agreement with the fold of r[(GGA)4]2, however, subtle differences are found in the region responsible for PrPC binding.

Ključne riječi
G-quadruplex; RNA; aptamer; NMR; GGA repeat; prion protein

Projekti
EC / FP7 / 261863 / BIO-NMR - NMR for Structural Biology

Hrčak ID: 131524

URI
http://hrcak.srce.hr/131524

Posjeta: 474 *