Document Detail

Tilted peptides: a structural motif involved in protein membrane insertion?
MedLine Citation:
PMID:  18069746     Owner:  NLM     Status:  MEDLINE    
Tilted peptides are short hydrophobic protein fragments characterized by an asymmetric distribution of their hydrophobic residues when helical. They are able to interact with a hydrophobic/hydrophilic interface (such as a lipid membrane) and to destabilize the organized system into which they insert. They were detected in viral fusion proteins and in proteins involved in different biological processes involving membrane insertion or translocation of the protein in which they are found. In this paper, we have analysed different protein domains related to membrane insertion with regard to their tilted properties. They are the N-terminal signal peptide of the filamentous haemagglutinin (FHA), a Bordetella pertussis protein secreted in high amount and the hydrophobic domain from proteins forming pores (i.e. ColIa, Bax and Bcl-2). From the predictions and the experimental approaches, we suggest that tilted peptides found in those proteins could have a more general role in the mechanism of insertion/translocation of proteins into/across membranes. For the signal sequences, they could help the protein machinery involved in protein secretion to be more active. In the case of toroidal pore formation, they could disturb the lipids, facilitating the insertion of the other more hydrophilic helices.
L Lins; R Brasseur
Related Documents :
17543216 - Water channel proteins: from their discovery in 1985 in cluj-napoca, romania, to the 20...
1848866 - The identification of proteins in the proximity of signal-anchor sequences during their...
18253086 - A novel mammalian trans-membrane protein reveals an alternative initiation pathway for ...
19549836 - Molecular mechanism of membrane constriction and tubulation mediated by the f-bar prote...
15123246 - Simultaneous characterization of the reductive unfolding pathways of rnase b isoforms b...
2464206 - Methods for staining amyloid in tissues: a review.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of peptide science : an official publication of the European Peptide Society     Volume:  14     ISSN:  1075-2617     ISO Abbreviation:  J. Pept. Sci.     Publication Date:  2008 Apr 
Date Detail:
Created Date:  2008-03-25     Completed Date:  2008-06-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9506309     Medline TA:  J Pept Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  416-22     Citation Subset:  IM    
Centre de Biophysique Moléculaire Numérique, FSAGx, Belgium.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Adhesins, Bacterial / chemistry,  genetics,  metabolism
Amino Acid Motifs
Amino Acid Sequence
Bordetella pertussis / chemistry
Hemagglutinins / chemistry,  genetics,  metabolism
Lipid Bilayers / chemistry,  metabolism
Lipid Metabolism
Lipids / chemistry
Liposomes / chemistry
Mass Spectrometry
Membrane Proteins / metabolism*
Models, Molecular
Molecular Sequence Data
Peptide Fragments / chemistry*,  genetics,  metabolism*
Peptides / chemical synthesis,  chemistry*
Protein Binding
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
Reg. No./Substance:
0/Adhesins, Bacterial; 0/Hemagglutinins; 0/Lipid Bilayers; 0/Lipids; 0/Liposomes; 0/Membrane Proteins; 0/Peptide Fragments; 0/Peptides

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Investigating trial and treatment heterogeneity in an individual patient data meta-analysis of survi...
Next Document:  Coupling desorption electrospray ionisation and neutral desorption/extractive electrospray ionisatio...