A structural model for desmosine cross-linked peptides.
Desmosine-enriched peptides were isolated from a thermolysin digest of bovine ligamentum nuchae elastin and a partial sequence was determined. A 'two-cross-link' model is proposed in which a second cross-link, perhaps lysinonorleucine, joins two peptide chains approx. 35 amino acid residues removed from the desmosine. Implied in this model is a certain asymmetry or directionality which places restrictions on the 'sense' of the peptide chains (either always parallel or anti-parallel) in order to align the cross-linking sites. Imposing such restrictions raises the possibility of specific alignment of elastin precursor molecules by microfibrillar proteins and/or aligning peptides on the precursor molecules themselves.
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D003895:Desmosine; D004549:Elastin; D008958:Models, Molecular; D010446:Peptide Fragments; D013820:Thermolysin
D010446:Peptide Fragments; D003895:Desmosine; D004549:Elastin; D013820:Thermolysin