The laminin-binding domain of agrin is structurally related to N-TIMP-1
The laminin-binding domain of agrin is structurally related to N-TIMP-1
复制标题
agrin 的层粘连蛋白结合域在结构上与 N-TIMP-1 相关
DOI：
10.1038/90422
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
R. Kammerer
中科院分区：
文献类型：
--
作者：
J. Stetefeld;M. Jenny;T. Schulthess;R. Landwehr;B. Schumacher;S. Frank;M. Rüegg;J. Engel;R. Kammerer
Agrin is the key organizer of postsynaptic differentiation at the neuromuscular junction. This organization activity requires the binding of agrin to the synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA) domain, which mediates a high-affinity interaction with the coiled coil domain of laminins. Here, we report the crystal structure of chicken NtA at 1.6 Å resolution. The structure reveals that NtA harbors an oligosaccharide/oligonucleotide-binding fold with several possible sites for the interaction with different ligands. A high structural similarity of NtA with the protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1) supports the idea of additional functions of agrin besides synaptogenic activity.
DOI：
10.1111/j.1432-1033.1995.0788h.x
发表时间：
1995-06
期刊：
European journal of biochemistry
影响因子：
--
作者：
N. Budisa;Boris Steipe;P. Demange;C. Eckerskorn;J. Kellermann;R. Huber
通讯作者：
N. Budisa;Boris Steipe;P. Demange;C. Eckerskorn;J. Kellermann;R. Huber