1jc7: Difference between revisions

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[[Image:1jc7.jpg|left|200px]]<br /><applet load="1jc7" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1jc7.jpg|left|200px]]<br /><applet load="1jc7" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1jc7, resolution 2.73Å" />

'''The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1'''<br />

==Overview==

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 A 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.

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 A 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.

==About this Structure==

1JC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1JC7 OCA].

1JC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC7 OCA].

==Reference==

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[[Category: timp]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 18~~:06:~~10 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:02 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1jc7.jpg|left|200px]]<br /><applet load="1jc7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jc7.jpg|left|200px]]<br /><applet load="1jc7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jc7, resolution 2.73&Aring;" />
 '''The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1'''<br />
 ==Overview==
-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 A 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.
+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 A 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.
 ==About this Structure==
-JC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JC7 OCA].
+JC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC7 OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: timp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:06:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:02 2008''