Abstract
Nidogen, an invariant component of basement membranes, is a multifunctional protein that interacts with most other major basement membrane proteins. Here, we report the crystal structure of the mouse nidogen-1 G2 fragment, which contains binding sites for collagen IV and perlecan. The structure is composed of an EGF-like domain and an 11-stranded beta-barrel with a central helix. The beta-barrel domain has unexpected similarity to green fluorescent protein. A large surface patch on the beta-barrel is strikingly conserved in all metazoan nidogens. Site-directed mutagenesis demonstrates that the conserved residues are involved in perlecan binding.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Conserved Sequence
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Crystallography, X-Ray
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Disulfides / metabolism
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Glycosylation
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Green Fluorescent Proteins
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Heparan Sulfate Proteoglycans / metabolism*
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Ligands
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Luminescent Proteins / chemistry
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Membrane Glycoproteins / chemistry*
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism*
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Mice
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Models, Molecular
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Molecular Sequence Data
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Mutation / genetics*
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Peptide Fragments / chemistry*
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Peptide Fragments / genetics
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Peptide Fragments / metabolism*
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Sequence Alignment
Substances
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Disulfides
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Heparan Sulfate Proteoglycans
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Ligands
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Luminescent Proteins
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Membrane Glycoproteins
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Peptide Fragments
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nidogen
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perlecan
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Green Fluorescent Proteins