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Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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1437-4315
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Volume 386, Issue 8 (Aug 2005)

Issues

The NC1 dimer of human placental basement membrane collagen IV: does a covalent crosslink exist?

Manuel E. Than
  • Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany
/ Gleb P. Bourenkov
  • MPG-ASMB, Gruppe Proteindynamik, c/o DESY, Notkestr. 85, D-22603 Hamburg, Germany
/ Stefan Henrich
  • Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany
/ Karlheinz Mann
  • Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany
/ Wolfram Bode
  • Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany
Published Online: 2005-09-06 | DOI: https://doi.org/10.1515/BC.2005.089

Abstract

Triple-helical collagen IV protomers associate through their N- and C-termini, forming a three-dimensional network that provides basement membranes with mechanical strength. Within this network, the C-terminal non-collagenous (NC1) domains form tight dimeric junctions. Crystallographic analyses of isolated NC1 domains show two trimeric cap-like structures interacting via a large interface. Previously, for NC1 from human placenta type-IV collagen we described covalent α1-α1 and α2-α2 crosslinks between Met93 and Lys211 of opposing α1(IV) and α2(IV) NC1-chains, which further stabilize this interface and explain the occurrence of reduction-insensitive NC1-chain dimers. However, their existence was recently questioned, and we therefore analyzed NC1-domain dimers in more detail by biochemical and protein crystallographic methods. Short-exposure diffraction data show a clear electron density cross-connecting the respective residues, which gradually disappears with prolonged crystal irradiation. Sequence analyses of isolated tryptic peptides derived from denatured NC1 monomers and dimers indicate that only the dimers, but not the monomers, yield these chemically labile cross-linked peptides. These data clearly demonstrate the presence of reduction-resistant, but chemically and radiation-sensitive covalent crosslinks between the side chains of Met93 and Lys211 in human placenta type-IV collagen.

Keywords: collagen IV; crosslink; crystal structure; Edman analysis; NC1 domain

References

About the article

Corresponding author


Received: March 23, 2005

Accepted: June 2, 2005

Published Online: 2005-09-06

Published in Print: 2005-08-01



Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.089. Export Citation

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[2]
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ChemPhysChem, 2011, Volume 12, Number 17, Page 3449
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