Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1
Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1
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DOI：
10.1038/89683
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发表时间：
2001-07-01
期刊：
影响因子：
--
通讯作者：
Hohenester, E
中科院分区：
文献类型：
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作者：
Hopf, M;Göhring, W;Hohenester, E
Nidogen是基底膜的不变成分，是一种多功能蛋白，与大多数其他主要的基底膜蛋白相互作用。在这里，我们报道了小鼠Nidogen-L GZ片段的晶体结构，该片段包含与IV型胶原和Perlecan结合的部位。该结构由一个类EGF结构域和一个带有中心螺旋的II链β-桶组成。β-Barrel结构域与绿色荧光蛋白有出人意料的相似之处。在所有后生动物的氮中，贝塔桶上的一大块表面斑块是惊人地保守的。定点突变表明，保守的残基参与了Perlecan的结合。
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-l GZ fragment, which contains binding sites for collagen IV and perlecan. The structure is composed of an EGF-like domain and an Ii-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 nitrogens. Site-directed mutagenesis demonstrates that the conserved residues are involved in perlecan binding.