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 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.
Floquet
Nicolas
N
Laboratoire de Spectroscopies et Structures BioMoléculaires, UFR Sciences Exactes et Naturelles, Institut Fédératif de Recherches Biomolécules FR 53, Université de Reims Champagne-Ardenne, BP 1039, 51687 REIMS Cedex2, France.
Pepe
Antonietta
A
Dauchez
Manuel
M
Bochicchio
Brigida
B
Tamburro
Antonio M
AM
Alix
Alain J P
AJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002942:Circular Dichroism; D030562:Databases, Protein; D004220:Disulfides / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014333:Tropoelastin / Q000737:chemistry* / Q000378:metabolism*
D004220:Disulfides; D014333:Tropoelastin