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1jb3

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{{STRUCTURE_1jb3| PDB=1jb3 | SCENE= }}
{{STRUCTURE_1jb3| PDB=1jb3 | SCENE= }}
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'''The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1'''
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===The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11473262 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11473262}}
==About this Structure==
==About this Structure==
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[[Category: Ob-fold]]
[[Category: Ob-fold]]
[[Category: Timp]]
[[Category: Timp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:00:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 19:56:59 2008''

Revision as of 16:57, 1 July 2008

Template:STRUCTURE 1jb3

The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1

Template:ABSTRACT PUBMED 11473262

About this Structure

1JB3 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

The laminin-binding domain of agrin is structurally related to N-TIMP-1., Stetefeld J, Jenny M, Schulthess T, Landwehr R, Schumacher B, Frank S, Ruegg MA, Engel J, Kammerer RA, Nat Struct Biol. 2001 Aug;8(8):705-9. PMID:11473262

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