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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

MPG-Autoren
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Than,  M. E.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Henrich,  S.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Ries,  A.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Mann,  K.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Kühn,  K.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Timpl,  R.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Bourenkov,  G. P.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Bartunik,  H. D.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Bode,  W.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

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.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0010-6F34-1
Zusammenfassung
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.