1h4u: Difference between revisions

Revision as of 13:57, 21 February 2008

DOMAIN G2 OF MOUSE NIDOGEN-1

OverviewOverview

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.

About this StructureAbout this Structure

1H4U is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1., Hopf M, Gohring W, Ries A, Timpl R, Hohenester E, Nat Struct Biol. 2001 Jul;8(7):634-40. PMID:11427896

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-[[Image:1h4u.gif|left|200px]]<br /><applet load="1h4u" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1h4u, resolution 2.20&Aring;" />
 '''DOMAIN G2 OF MOUSE NIDOGEN-1'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-H4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4U OCA].
+H4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4U OCA].
 ==Reference==
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 [[Category: extracellular matrix protein]]
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