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A sulfilimine bond identified in collagen IV.

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.

SUBMITTER: Vanacore R

PROVIDER: S-EPMC2876822 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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A sulfilimine bond identified in collagen IV.

Vanacore Roberto R Ham Amy-Joan L AJ Voehler Markus M Sanders Charles R CR Conrads Thomas P TP Veenstra Timothy D TD Sharpless K Barry KB Dawson Philip E PE Hudson Billy G BG

Science (New York, N.Y.) 20090901 5945

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 ...[more]

PMID: 19729652

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Computational insights into the formation and nature of the sulfilimine bond in collagen-IV.

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