Radixin
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='77/777076/Cv/2'>hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule</scene>hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds<ref>PMID:18706570</ref>. {{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}} | + | The <scene name='77/777076/Cv/2'>hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule</scene> hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds<ref>PMID:18706570</ref>. {{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}} |
</StructureSection> | </StructureSection> | ||
== 3D Structures of radixin == | == 3D Structures of radixin == | ||
Revision as of 15:58, 10 July 2018
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3D Structures of radixin
Updated on 10-July-2018
1gc7, 2d2q – mRdx FERM domain – mouse
3x23, 2ems, 2yvc, 2d10, 2d11, 2emt, 1j19, 2zpy – mRdx FERM domain + peptide
1gc6 – mRdx FERM domain + inositol-triphosphate
References
- ↑ Valderrama F, Thevapala S, Ridley AJ. Radixin regulates cell migration and cell-cell adhesion through Rac1. J Cell Sci. 2012 Jul 15;125(Pt 14):3310-9. doi: 10.1242/jcs.094383. Epub 2012 Mar, 30. PMID:22467863 doi:http://dx.doi.org/10.1242/jcs.094383
- ↑ Tachibana K, Haghparast SM, Miyake J. Inhibition of cell adhesion by phosphorylated Ezrin/Radixin/Moesin. Cell Adh Migr. 2015;9(6):502-12. doi: 10.1080/19336918.2015.1113366. PMID:26555866 doi:http://dx.doi.org/10.1080/19336918.2015.1113366
- ↑ Kikuchi S, Hata M, Fukumoto K, Yamane Y, Matsui T, Tamura A, Yonemura S, Yamagishi H, Keppler D, Tsukita S, Tsukita S. Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. Nat Genet. 2002 Jul;31(3):320-5. doi: 10.1038/ng905. Epub 2002 Jun 17. PMID:12068294 doi:http://dx.doi.org/10.1038/ng905
- ↑ . PMID:18706570
