1jb3
From Proteopedia
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- | [[ | + | ==The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1== |
+ | <StructureSection load='1jb3' size='340' side='right' caption='[[1jb3]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1jb3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JB3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JB3 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jb3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jb3 RCSB], [http://www.ebi.ac.uk/pdbsum/1jb3 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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<ref>PMID:11473262</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Agrin|Agrin]] | *[[Agrin|Agrin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Stetefeld, J.]] | [[Category: Stetefeld, J.]] |
Revision as of 11:49, 28 September 2014
The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1
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