In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1-20 is flexibly disordered, and residues 21-143 adopt the same globular fold as in mature SCP2.
Cell Mol Life Sci
; 54(7): 751-9, 1998 Jul.
Article
en En
| MEDLINE
| ID: mdl-9711242
ABSTRACT
The preform of the rabbit sterol carrier protein 2 (pre-rSCP2) was cloned, the uniformly 15N-labelled protein expressed in Escherichia coli and studied by three-dimensional 15N-resolved nuclear magnetic resonance spectroscopy. In spite of its low solubility in aqueous solution of only approximately 0.3 mM, sequential 15N and 1H backbone resonance assignments were obtained for 105 out of the 143 residues. From comparison of the sequential and medium-range nuclear Overhauser effects (NOEs) in the two proteins, all regular secondary structures previously determined in mature human SCP2 (hSCP2) [Szyperski et al. (1993) FEBS Lett. 335 18-26] were also identified in pre-rSCP2. Near-identity of the backbone 15N and 1H chemical shifts and 11 correspondence of 24 long-range NOEs to backbone amide groups in the two proteins show that the residues 21-143 adopt the same globular fold in pre-rSCP2 and mature hSCP2. The N-terminal 20-residue leader peptide of pre-rSCP2 is flexibly disordered in solution and does not observably affect the conformation of the polypeptide segment 21-143.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Precursores de Proteínas
/
Señales de Clasificación de Proteína
/
Pliegue de Proteína
/
Proteínas de Ciclo Celular
/
Proteínas de Unión al ADN
Límite:
Animals
Idioma:
En
Revista:
Cell Mol Life Sci
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
1998
Tipo del documento:
Article
País de afiliación:
Suiza