Structural and Binding Study of Modified siRNAs with the Agonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Jan 5;
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute 2 protein of Drosophila melanogaster was also studied. The structures show that the modified siRNA duplexes (ANA/RNA) adopt a geometry very similar to the naturally occurring A-type siRNA duplex. All ribose residues, except for the 3' overhang, show 3'-endo conformation. The six-membered altritol sugar in ANA occurs in a chair conformation with the nucleobase in an axial position. In all siRNA duplexes, two overhanging nucleotides at the 3' end enhance the stability of the first neighboring base pair by a stacking interaction. The first overhanging nucleotide has a rather fixed position, whereas the second overhanging nucleotide shows larger flexibility. NMR binding studies of the PAZ domain with ANA-modified siRNAs demonstrate that modifications in the double-stranded region of the antisense strand have some small effects on the binding affinity as compared with the unmodified siRNA. Modification of the 3' overhang with thymidine (dTdT) residues shows a sixfold increase in the binding affinity compared with the unmodified siRNA (relative binding affinity of 17 % compared with dTdT-modified overhang), whereas modification of the 3' overhang with ANA largely decreases the binding affinity.
PMID: 21207526 [PubMed - as supplied by publisher]
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Structural and Binding Study of Modified siRNAs with the Argonaute 2 PAZ Domain by NMR Spectroscopy.
Chemistry. 2011 Feb 1;17(5):1519-1528
Authors: Maiti M, Nauwelaerts K, Lescrinier E, Herdewijn P
By using high-resolution NMR spectroscopy, the structures of a natural short interfering RNA (siRNA) and of several altritol nucleic acid (ANA)-modified siRNAs were determined. The interaction of modified siRNAs with the PAZ domain of the Argonaute...
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01-27-2011 02:52 PM
[NMR paper] NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: c
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Biochemistry. 2005 Mar 15;44(10):3708-17
Authors: Volpon L, D'Orso I, Young CR, Frasch AC, Gehring K
TcUBP1 is a trypanosome cytoplasmic RNA-binding protein containing a single, conserved RNA-recognition motif (RRM) domain involved in selective destabilization of U-rich...
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11-24-2010 11:14 PM
[NMR paper] NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding
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Chembiochem. 2003 Sep 5;4(9):870-7
Authors: Dehner A, Furrer J, Richter K, Schuster I, Buchner J, Kessler H
Hsp90 is one of the most abundant chaperone proteins in the cytosol. In an ATP-dependent manner it plays an essential role in the folding and activation of a...
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11-24-2010 09:16 PM
[NMR paper] Proton NMR study of chemically modified horse heart ferricytochrome c confirms the pr
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J Inorg Biochem. 2003 Apr 1;94(4):381-5
Authors: Sivakolundu SG, Mabrouk PA
Comparison of the 1H NMR spectra for guanidinated ferricyt c and chloro(terpyridine)platinum(II)-modified ferricyt c in 30%...
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11-24-2010 09:01 PM
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J Biol Chem. 2001 Jul 6;276(27):25150-6
Authors: Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buée L, Lippens G, Landrieu I
The recent crystal structure of Pin1 protein bound to a doubly phosphorylated peptide from the C-terminal domain of RNA polymerase II revealed that binding interactions between Pin1 and its substrate take place through its...
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11-19-2010 08:32 PM
[NMR paper] NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9.
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Protein Sci. 1999 Aug;8(8):1711-3
Authors: Hannan JP, Whittaker SB, Davy SL, Kühlmann UC, Pommer AJ, Hemmings AM, James R, Kleanthous C, Moore GR
Ni2+ affinity columns are widely used for protein purification, but they carry the risk that Ni2+ ions may bind to the protein, either adventitiously or at a physiologically important site. Dialysis against ethylenediaminetetraacetic acid...
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11-18-2010 08:31 PM
[NMR paper] The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and
The binding of 5-fluorouracil to native and modified human serum albumin: UV, CD, and 1H and 19F NMR investigation.
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J Pharm Biomed Anal. 1995 Aug;13(9):1087-93
Authors: Bertucci C, Ascoli G, Uccello-Barretta G, Di Bari L, Salvadori P
5-Fluorouracil (FU) is an important and widely used antineoplastic drug...