1LI1

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

Summary for 1LI1

• Entry DOI: 10.2210/pdb1li1/pdb
• Descriptor: Collagen alpha 1(IV), Collagen alpha 2(IV), ACETATE ION, ... (4 entities in total)
• Functional Keywords: basement membrane, collagen iv, nc1 domain, covalent cross-link, protein-protein interaction, structural protein
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted, extracellular space, extracellular matrix, basement membrane: P02462 P08572
• Total number of polymer chains: 6
• Total formula weight: 152187.98

Authors

Than, M.E.,Henrich, S.,Huber, R.,Ries, A.,Mann, K.,Kuhn, K.,Timpl, R.,Bourenkov, G.P.,Bartunik, H.D.,Bode, W. (deposition date: 2002-04-17, release date: 2002-05-22, Last modification date: 2024-10-09)

Primary citation

Than, M.E.,Henrich, S.,Huber, R.,Ries, A.,Mann, K.,Kuhn, K.,Timpl, R.,Bourenkov, G.P.,Bartunik, H.D.,Bode, W.
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.
Proc.Natl.Acad.Sci.USA, 99:6607-6612, 2002

PubMed 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-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.

PubMed: 12011424
DOI: 10.1073/pnas.062183499

Experimental method

X-RAY DIFFRACTION (1.9 Å)