1H4U

Domain G2 of mouse nidogen-1

Summary for 1H4U

• Entry DOI: 10.2210/pdb1h4u/pdb
• Descriptor: NIDOGEN-1 (2 entities in total)
• Functional Keywords: extracellular matrix protein
• Biological source: MUS MUSCULUS (MOUSE)
• Cellular location: Secreted, extracellular space, extracellular matrix, basement membrane: P10493
• Total number of polymer chains: 1
• Total formula weight: 29272.76

Authors

Hopf, M.,Gohring, W.,Ries, A.,Timpl, R.,Hohenester, E. (deposition date: 2001-05-14, release date: 2001-06-28, Last modification date: 2024-11-06)

Primary citation

Hopf, M.,Gohring, W.,Ries, A.,Timpl, R.,Hohenester, E.
Crystal Structure and Mutational Analysis of a Perlecan-Binding Fragment of Nidogen-1
Nat.Struct.Biol., 8:634-, 2001

PubMed 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.

PubMed: 11427896
DOI: 10.1038/89683

Experimental method

X-RAY DIFFRACTION (2.2 Å)