1jb3: Difference between revisions

Revision as of 19:57, 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:1jb3.png

Template:STRUCTURE 1jb3

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

1JB3 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 19:56:59 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jb3.jpg|left|200px]]
+{{Seed}}
+[[Image:1jb3.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1jb3|  PDB=1jb3  |  SCENE=  }}
-'''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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11473262}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11473262 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11473262}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Ob-fold]]
 [[Category: Timp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:00:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 19:56:59 2008''