RT info:eu-repo/semantics/article
T1 Primary sequence and 3D structure prediction of the plant toxin stenodactylin
A1 Iglesias Álvarez, María del Rosario
A1 Polito, Letizia
A1 Bortolotti, Massimo
A1 Pedrazzi, Manuela
A1 Citores González, Lucía
A1 Ferreras Rodríguez, José Miguel
A1 Bolognesi, Andrea
K1 Proteins - Synthesis
K1 Proteínas
K1 Ribosomes - Structure
K1 3D structure
K1 Plant toxin
K1 Primary sequence
K1 Ribosome-inactivating
protein
K1 Stenodactylin
K1 3209 Farmacología
K1 3214 Toxicología
AB Stenodactylin is one of the most potent type 2 ribosome-inactivating proteins (RIPs); its high toxicity has been demonstrated in several models both in vitro and in vivo. Due to its peculiarities, stenodactylin could have several medical and biotechnological applications in neuroscience and cancer treatment. In this work, we report the complete amino acid sequence of stenodactylin and 3D structure prediction. The comparison between the primary sequence of stenodactylin and other RIPs allowed us to identify homologies/differences and the amino acids involved in RIP toxic activity. Stenodactylin RNA was isolated from plant caudex, reverse transcribed through PCR and the cDNA was amplificated and cloned into a plasmid vector and further analyzed by sequencing. Nucleotide sequence analysis showed that stenodactylin A and B chains contain 251 and 258 amino acids, respectively. The key amino acids of the active site described for ricin and most other RIPs are also conserved in the stenodactylin A chain. Stenodactylin amino acid sequence shows a high identity degree with volkensin (81.7% for A chain, 90.3% for B chain), whilst when compared with other type 2 RIPs the identity degree ranges from 27.7 to 33.0% for the A chain and from 42.1 to 47.7% for the B chain.
PB MDPI
SN 2072-6651
YR 2020
FD 2020
LK https://uvadoc.uva.es/handle/10324/58968
UL https://uvadoc.uva.es/handle/10324/58968
LA eng
NO Toxins, 2020, Vol. 12, Nº. 9, 538
NO Producción Científica
DS UVaDOC
RD 19-oct-2024