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    Nat Struct Biol. 2001 Jul;8(7):634-40.

    Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.

    Hopf M, Göhring W, Ries A, Timpl R, Hohenester E.

    Abteilung Proteinchemie, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany.

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    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.

    PMID: 11427896 [PubMed - indexed for MEDLINE]

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