Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
FEBS Lett
; 505(3): 431-5, 2001 Sep 21.
Article
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| MEDLINE
| ID: mdl-11576542
ABSTRACT
PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively charged. The conformational coupling between the transmembrane span and the cytoplasmic domain of PMP1 was investigated from 1H-nuclear magnetic resonance data of two synthetic fragments F9-F38, i.e. 80% of the whole sequence, and Y25-F38, the isolated cytoplasmic domain. Highly disordered in aqueous solution, the Y25-F38 peptide adopts a well-defined conformation in the presence of dodecylphosphocholine micelles. Compared with the long PMP1 fragment, this structure exhibits both native and non-native elements. Our results make it possible to assess the influence of a hydrophobic anchor on the intrinsic conformational propensity of a cytoplasmic domain.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteolípidos
/
Proteínas de la Membrana
Idioma:
En
Revista:
FEBS Lett
Año:
2001
Tipo del documento:
Article
País de afiliación:
Francia