IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
A peptide recognition event leading to the native fold of E. coli thioredoxin: an NMR study
Autor/es:
JAVIER SANTOS; ANDRÉS BINOLFI; CLAUDIO FERNÁNDEZ; JOSÉ MARÍA DELFINO
Lugar:
USA, Boston
Reunión:
Congreso; Biophysical Society (USA) 2009; 2009
Resumen:
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A peptide recognition event leading to the
native fold of E. coli thioredoxin: an NMR study
Javier Santos 1,
Andrés Binolfi2, Claudio Fernández2, and José M.
Delfino1
1Departmento
de Química Biológica e Instituto de Química y Fisicoquímica Biológicas
(IQUIFIB), Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires,
Junín 956, C1113AAD, Buenos Aires, Argentina.
2Instituto
de Biología Molecular y Celular de Rosario, Consejo Nacional de Investigaciones
Científicas y Técnicas, Universidad Nacional de Rosario, Suipacha 531,
S2002LRK, Rosario, Argentina.
To whom correspondence should be addressed. E-mail:
jsantos@qb.ffyb.uba.ar delfino@qb.ffyb.uba.ar
The reduced form of fragment 1-93 of E. coli
thioredoxin (TRX1-93) adopts in solution a partially folded conformation that
consolidates into a native-like state upon interaction with peptide TRX94-108.
A functional complex is formed spontaneously upon mixing both partners (Santos
et al. 2007 Biochemistry 46, 5148-5159). Because isolated peptide TRX94-108
remains unstructured in solution and fragment TRX1-93 exhibits features of a
molten globule state, folding of both peptide and fragment should occur
concomitantly. We have recently shown that specific interactions involving L99,
F102 and L103 between peptide TRX94-108 and partially folded TRX1-93 play a key
role in stabilizing the native-like tertiary structure of the complex (Santos
et al. 2009 Biochemistry 48, 595-607). In this context, we hypothesize that
folding depends on the formation of a cooperative tertiary unit based on the
interaction between a-helix 5 of peptide TRX94-108 and a-helix 3 of fragment
TRX1-93. This view is supported by results from molecular dynamics simulations.
Here we report an NMR-based approach aimed at uncovering the molecular events
leading to complex formation.