A Sulfilimine Bond Identified in Collagen IV-Reference-Cited by-同舟云学术

A Sulfilimine Bond Identified in Collagen IV

Published:2009-09-04 Issue:5945 Volume:325 Page:1230-1234
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Vanacore Roberto¹,Ham Amy-Joan L.²,Voehler Markus³,Sanders Charles R.²,Conrads Thomas P.⁴,Veenstra Timothy D.⁴,Sharpless K. Barry⁵,Dawson Philip E.⁵⁶,Hudson Billy G.¹²⁷

Affiliation:

1. Division of Nephrology, Department of Medicine and Center for Matrix Biology, Vanderbilt University, Nashville, TN 37232, USA.

2. Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, USA.

3. Department of Chemistry, Vanderbilt University, Nashville, TN 37232, USA.

4. Laboratory of Proteomics and Analytical Technologies, Advanced Technology Program, SAIC-Frederick, Incorporated, National Cancer Institute, Frederick, MD 21702, USA.

5. Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

6. Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

7. Department of Pathology, Vanderbilt University, Nashville, TN 37232, USA.

Abstract

Toughing It Out in Membranes The formation of crosslinks in the triple-helical structure of collagen is crucial to its function. In the case of collagen IV, which provides structural integrity to the basement membrane of animal tissues, the chemical nature of the crosslinks has been difficult to pin down. Vanacore et al. (p. 1230 ) report a combination of high-resolution mass spectrometric and nuclear magnetic resonance studies that establish the crosslink between hydroxylysine-211 and methionine-93 is a sulfimine group (-S=N-). This type of bond appears to have evolved to withstand mechanical stress as animals evolved into more structurally complex organisms.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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