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Titolo:
Folding of a dimeric beta-barrel: Residual structure in the urea denaturedstate of the human papillomavirus E2 DNA binding domain
Autore:
Mok, YK; Alonso, LG; Lima, LMTR; Bycroft, M; De Prat-Gay, G;
Indirizzi:
Univ Buenos Aires, Fac Ciencias Exactas & Nat, Fdn Campomar, Inst Invest Bioquim, RA-1405 Buenos Aires, DF, Argentina Univ Buenos Aires Buenos AiresDF Argentina RA-1405 Aires, DF, Argentina Univ Cambridge, Chem Lab, MRC Unit Prot Funct & Design, Cambridge CB2 1EW,England Univ Cambridge Cambridge England CB2 1EW sign, Cambridge CB2 1EW,England Univ Fed Rio de Janeiro, Dept Bioquim Med, BR-21914590 Rio De Janeiro, Brazil Univ Fed Rio de Janeiro Rio De Janeiro Brazil BR-21914590 BCeiro, Brazil
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 4, volume: 9, anno: 2000,
pagine: 799 - 811
SICI:
0961-8368(200004)9:4<799:FOADBR>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPIN COUPLING-CONSTANTS; AMINO-TERMINAL DOMAIN; CHEMICAL-SHIFTS; NMR-SPECTROSCOPY; IMPROVED SENSITIVITY; H-1-NMR ASSIGNMENTS; SOLVENT SUPPRESSION; HETERONUCLEAR NMR; CRYSTAL-STRUCTURE; FOLDED PROTEINS;
Keywords:
dimer; DNA binding; E2; folding; urea-denatured state;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: De Prat-Gay, G Univ Buenos Aires, Fac Ciencias Exactas & Nat, Fdn Campomar, Inst Invest Bioquim, Patricias Argentinas 435, RA-1405 Buenos Aires, DF, Argentina Univ Buenos Aires Patricias Argentinas 435 Buenos Aires DF Argentina RA-1405
Citazione:
Y.K. Mok et al., "Folding of a dimeric beta-barrel: Residual structure in the urea denaturedstate of the human papillomavirus E2 DNA binding domain", PROTEIN SCI, 9(4), 2000, pp. 799-811

Abstract

The dimeric beta-barrel is a characteristic topology initially found in the transcriptional regulatory domain of the E2 DNA binding domain from papillomaviruses. We have previously described the kinetic folding mechanism of the human HPV-16 domain, and, as part of these studies, we present a structural characterization of the urea-denatured state of the protein. We have obtained a set of chemical shift assignments for the C-terminal domain in urea using heteronuclear NMR methods and found regions with persistent residual structure. Based on chemical shift deviations from random coil values, (3)J(NHN alpha) coupling constants, heteronuclear single quantum coherence peak intensities, and nuclear Overhauser effect data, we have determined clusters of residual structure in regions corresponding to the DNA binding helix and the second beta-strand in the folded conformation. Most of the structures found are of nonnative nature, including turn-like conformations. Urea denaturation at equilibrium displayed a loss in protein concentration dependence, in absolute parallel to a similar deviation observed in the folding rate constant from kinetic experiments. These results strongly suggest analternative folding pathway in which a dimeric intermediate is formed and the rate-limiting step becomes first order at high protein concentrations. The structural elements found in the denatured state would collide to yieldproductive interactions, establishing an intermolecular folding nucleus athigh protein concentrations. We discuss our results in terms of the folding mechanism of this particular topology in an attempt to contribute to a better understanding of the folding of dimers in general and intertwined dimeric proteins such as transcription factors in particular.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 19:11:20