Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1
| Autor: | M, Hopf, W, Göhring, A, Ries, R, Timpl, E, Hohenester |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Binding Sites Glycosylation Membrane Glycoproteins Green Fluorescent Proteins Molecular Sequence Data Crystallography X-Ray Ligands Peptide Fragments Protein Structure Secondary Protein Structure Tertiary Luminescent Proteins Mice Mutation Animals Amino Acid Sequence Disulfides Sequence Alignment Conserved Sequence Heparan Sulfate Proteoglycans Protein Binding |
| Zdroj: | Nature structural biology. 8(7) |
| ISSN: | 1072-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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