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Titolo:
NF-kappa B binding mechanism: A nuclear magnetic resonance and modeling study of a GGG -> CTC mutation
Autore:
Tisne, C; Hartmann, B; Delepierre, M;
Indirizzi:
Inst Pasteur, Lab RMN, CNRS URA 1129, F-75015 Paris, France Inst Pasteur Paris France F-75015 , CNRS URA 1129, F-75015 Paris, France Inst Biol Physicochim, CNRS UPR 9080, Biochim Lab, F-75005 Paris, France Inst Biol Physicochim Paris France F-75005 im Lab, F-75005 Paris, France
Titolo Testata:
BIOCHEMISTRY
fascicolo: 13, volume: 38, anno: 1999,
pagine: 3883 - 3894
SICI:
0006-2960(19990330)38:13<3883:NBBMAN>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; NMR COUPLING-CONSTANTS; P-31 NMR; P50 HOMODIMER; MOLECULAR SIMULATION; DNA OLIGONUCLEOTIDES; PHOSPHATE BACKBONE; FORCE-FIELD; CONFORMATION; SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Delepierre, M Inst Pasteur, Lab RMN, CNRS URA 1129, 28 Rue Dr Roux, F-75015 Paris, France Inst Pasteur 28 Rue Dr Roux Paris France F-75015 is, France
Citazione:
C. Tisne et al., "NF-kappa B binding mechanism: A nuclear magnetic resonance and modeling study of a GGG -> CTC mutation", BIOCHEM, 38(13), 1999, pp. 3883-3894

Abstract

We present the solution structure of the nonpalindromic 16 bp DNA (5')d(CTGCTCACTTTCCAGG)(3'). (5')d(CCTGGAAAGTGAGCAG) (3') containing a mutated kappa B Site for which the mutation of a highly conserved GGG tract of the native kappa B HIV-1 site to CTC abolishes NF-kappa B binding. H-1 and P-31 NMRspectroscopies have been used together with molecular modeling to determine the fine structure of the duplex. NMR data show evidence for a BI-BII equilibrium of the CpA.TpG steps at the 3'-end of the oligomer. Models for theextreme conformations reached by the mutated duplex (denoted 16M) are proposed in agreement with the NMR data. Since the distribution of BII sites ischanged in the mutated duplex compared to that of the native duplex (denoted 16N), large differences are induced in the intrinsic structural properties of both duplexes. in particular, in BII structures, 16M shows a kink located at the 3'-end of the duplex, and in contrast, 16N exhibits an intrinsic global curvature toward the major groove. Whereas 16N can reach a conformation very favorable for the interaction with NF-kappa B, 16M cannot mimic such a conformation and, moreover, its deeper and narrower major groove could hinder the DNA-protein interactions.

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Documento generato il 12/08/20 alle ore 20:05:44