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  The 1.9-angstrom crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link

Than, M. E., Henrich, S., Huber, R., Ries, A., Mann, K., Kühn, K., et al. (2002). The 1.9-angstrom crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proceedings of the National Academy of Sciences of the United States of America, 99(10), 6607-6612.

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Genre: Journal Article
Alternative Title : Proc. Natl. Acad. Sci. U. S. A.

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 Creators:
Than, M. E.1, Author           
Henrich, S.1, Author           
Huber, R.1, Author           
Ries, A.2, Author           
Mann, K.1, 3, Author           
Kühn, K.1, Author           
Timpl, R.2, Author           
Bourenkov, G. P.1, Author           
Bartunik, H. D.1, Author           
Bode, W.1, 4, 5, Author           
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              
3Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
4Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
5Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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 Abstract: Triple-helical collagen IV protomers associate through their N- and C-termini forming a three-dimensional network, which provides basement membranes with an anchoring scaffold and mechanical strength. The noncollagenous (NC1) domain of the C- terminal junction between two adjacent collagen IV protomers from human placenta was crystallized and its 1.9-Angstrom structure was solved by multiple anomalous diffraction (MAD) phasing, This hexameric NC1 particle is composed of two trimeric caps, which interact through a large planar interface. Each cap is formed by two alpha1 fragments and one alpha2 fragment with a similar previously uncharacterized fold, segmentally arranged around an axial tunnel. Each monomer chain folds into two structurally very similar subdomains, which each contain a finger-like hairpin loop that inserts into a six- stranded beta-sheet of the neighboring subdomain of the same or the adjacent chain. Thus each trimer forms a quite regular, but non-classical, sixfold propeller. The trimer-trimer interaction is further stabilized by a previously uncharacterized type of covalent cross-link between the side chains of a Met and a Lys residue of the alpha1 and alpha2 chains from opposite trimers, explaining previous findings of nonreducible cross-links in NC1. This structure provides insights into NC1-related diseases such as Goodpasture and Alport syndromes.

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Language(s): eng - English
 Dates: 2002-05-14
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41117
ISI: 000175637300019
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 99 (10) Sequence Number: - Start / End Page: 6607 - 6612 Identifier: ISSN: 0027-8424