Pharmaceutical Sciences Faculty Publications
A Sulfilimine Bond Identified in Collagen IV
Document Type
Article
Publication Date
9-4-2009
Journal Title
Science
ISSN
1095-9203
Volume
325
Issue
5945
First Page
1230
Last Page
1234
DOI
10.1126/science.1176811
PubMed ID
19729652
PubMed Central® ID
PMC2876822
Abstract
Collagen IV networks are ancient proteins of basement membranes that underlie epithelia in metazoa from sponge to human. The networks provide structural integrity to tissues and serve as ligands for integrin cell-surface receptors. They are assembled by oligomerization of triple-helical protomers and are covalently crosslinked, a key reinforcement that stabilizes networks. We used Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules. This bond, the nitrogen analog of a sulfoxide, appears to have arisen at the divergence of sponge and cnidaria, an adaptation of the extracellular matrix in response to mechanical stress in metazoan evolution.
Keywords
Amino acid sequence, collagen type IV, mass spectrometry, biomolecular, protein
Recommended Citation
Vanacore, Roberto; Ham, Amy-Joan L.; Voehler, Markus; Sanders, Charles R.; Conrads, Thomas P.; Veenstra, Timothy D.; Sharpless, K. Barry; Dawson, Philip E.; and Hudson, Billy G., "A Sulfilimine Bond Identified in Collagen IV" (2009). Pharmaceutical Sciences Faculty Publications. 294.
https://digitalcommons.cedarville.edu/pharmaceutical_sciences_publications/294
