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1li1

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1li1, resolution 1.90Å

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

Contents

Overview

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-A 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, alpha 1 fragments and one alpha 2 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 nonclassical, 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 alpha 1 and alpha 2 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.

Disease

Known diseases associated with this structure: Brain small vessel disease with hemorrhage OMIM:[120130], Porencephaly OMIM:[120130]

About this Structure

1LI1 is a Protein complex structure of sequences from Homo sapiens with ACT as ligand. Full crystallographic information is available from OCA.

Reference

The 1.9-A 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 ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W, Proc Natl Acad Sci U S A. 2002 May 14;99(10):6607-12. PMID:12011424

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