1jc7: Difference between revisions

Revision as of 20:00, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jc7.png

Template:STRUCTURE 1jc7

The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1

Template:ABSTRACT PUBMED 11473262

About this StructureAbout this Structure

1JC7 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 20:00:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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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