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| <StructureSection load='3i70' size='350' side='right' caption='Chicken agrin (PDB code [[3i70]]).' scene='41/417482/Cv/2'> | | <StructureSection load='' size='350' side='right' caption='Chicken agrin (PDB code [[3i70]]).' scene='41/417482/Cv/2'> |
| __TOC__ | | __TOC__ |
| == Function == | | == Function == |
Revision as of 12:34, 13 December 2017
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Function
Agrin (Agr) is involved in the embryogenesis of the neuromuscular junction. It is involved in the aggregation of acetylcholine receptors. [1]
Relevance
Agr is an inducer of mammalian heart regeneration[2].
Disease
Agr is overexpressed in brains of Alzheimer Disease patients. Agr is associated with myasthenic syndrome.
Structural highlights
Agr N-terminal domain binds laminin. The C-terminal of Agr has 3 laminin-like globular domains (LMB) G1-G3 and 4 epidermal growth factor-like domains. Agr binds heparan sulfate post-translationally. Other Agr domains are: Kazal type serine protease inhibitor.
- ↑ Tsen G, Halfter W, Kroger S, Cole GJ. Agrin is a heparan sulfate proteoglycan. J Biol Chem. 1995 Feb 17;270(7):3392-9. PMID:7852425
- ↑ Bassat E, Mutlak YE, Genzelinakh A, Shadrin IY, Baruch Umansky K, Yifa O, Kain D, Rajchman D, Leach J, Riabov Bassat D, Udi Y, Sarig R, Sagi I, Martin JF, Bursac N, Cohen S, Tzahor E. The extracellular matrix protein agrin promotes heart regeneration in mice. Nature. 2017 Jul 13;547(7662):179-184. doi: 10.1038/nature22978. Epub 2017 Jun 5. PMID:28581497 doi:https://dx.doi.org/10.1038/nature22978
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3D Structures of Agrin
Updated on 13-December-2017
3i70, 1pxu – cNtA – chicken
1pz7, 1pz8, 1pz9 – cAgr
1q56 – cAgr LMB G3+Ca – NMR
1jb3, 1jc7 – cAgr LMB
3pve – Agr LMB G2 - mouse
3v65, 3v64 – Agr LMB G3 + Low-density lipoprotein receptor-related protein 4 - rat
References
