Nature Structural Biology
8, 634 - 640 (2001)
doi:10.1038/89683
Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1Michael Hopf1, Walter Göhring1, Albert Ries1, Rupert Timpl1
& Erhard Hohenester2, 31
Abteilung Proteinchemie, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany. 2
Biophysics Section, Blackett Laboratory, Imperial College, Prince Consort Road, London SW7 2BW, UK. 3
Division of Medicine, Imperial College School of Medicine, Exhibition Road, London SW7 2AZ, UK.
Correspondence should be addressed to Erhard Hohenester e.hohenester@ic.ac.ukNidogen, 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  -barrel with a central helix. The -barrel domain has unexpected similarity to green fluorescent protein. A large surface patch on the -barrel is strikingly conserved in all metazoan nidogens. Site-directed mutagenesis demonstrates that the conserved residues are involved in perlecan binding.
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