Agrin
From Proteopedia
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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. | 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. | ||
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| + | == 3D Structures of Agrin == | ||
| + | [[Agrin 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
Revision as of 11:04, 3 March 2019
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3D Structures of Agrin
Updated on 03-March-2019
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
- ↑ 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:http://dx.doi.org/10.1038/nature22978
