Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.
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.
Hopf
M
M
Abteilung Proteinchemie, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
Göhring
W
W
Ries
A
A
Timpl
R
R
Hohenester
E
E
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004220:Disulfides / Q000378:metabolism; D006031:Glycosylation; D049452:Green Fluorescent Proteins; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism*; D008024:Ligands; D008164:Luminescent Proteins / Q000737:chemistry; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics*; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D004220:Disulfides; D019812:Heparan Sulfate Proteoglycans; D008024:Ligands; D008164:Luminescent Proteins; D008562:Membrane Glycoproteins; D010446:Peptide Fragments; C029967:nidogen; C071927:perlecan; D049452:Green Fluorescent Proteins