Structure and modeling studies of the carboxy-terminus region of human tropoelastin

Elastin macromolecular assembly is a highly complex mechanism involving many steps including coacervation, cross-linking, and probably other (not known) phenomena. In past studies, it has been proposed that the C-terminal part of tropoelastin is also involved in this process and may play a key role...

Full description

Saved in:
Bibliographic Details
Published in:Matrix biology 2005-06, Vol.24 (4), p.271-282
Main Authors: Floquet, Nicolas, Pepe, Antonietta, Dauchez, Manuel, Bochicchio, Brigida, Tamburro, Antonio M., Alix, Alain J.P.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Circular Dichroism
Consensus sequence
Databases, Protein
Disulfides - metabolism
Elastin structure
Humans
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular modeling
Molecular Sequence Data
Monte Carlo Method
NMR
Peptide assembly
Protein Structure, Tertiary
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tropoelastin - chemistry
Tropoelastin - metabolism
Tropoelastin exon 36
β-turns
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Elastin macromolecular assembly is a highly complex mechanism involving many steps including coacervation, cross-linking, and probably other (not known) phenomena. In past studies, it has been proposed that the C-terminal part of tropoelastin is also involved in this process and may play a key role in tropoelastin interactions with other proteins of the final elastic fibres scaffold. Presented here are the results of the biophysical studies (biospectroscopy, bioinformatics) of the C-terminal domain of tropoelastin. We report the detailed structures adopted by the oxidized (native) and reduced forms of the free synthetic peptide with sequence encoded by exon 36 of human tropoelastin (GGACLGKACGRKRK) and propose a dynamical interpretation of which structures may be involved in interactions with other extra-cellular matrix proteins. We also suggest that these structures may be retrieved in other proteins sharing a consensus sequence; however no definitive conclusion can be drawn here on a possible structure–function relationship.
ISSN:0945-053X
1569-1802
DOI:10.1016/j.matbio.2005.03.002