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| | <StructureSection load='5jia' size='340' side='right'caption='[[5jia]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5jia' size='340' side='right'caption='[[5jia]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jia]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JIA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jia]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JIA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ji7|5ji7]], [[5ji9|5ji9]], [[5jiu|5jiu]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ranbp10, Kiaa1464 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jia OCA], [https://pdbe.org/5jia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jia RCSB], [https://www.ebi.ac.uk/pdbsum/5jia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jia ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jia OCA], [http://pdbe.org/5jia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jia RCSB], [http://www.ebi.ac.uk/pdbsum/5jia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jia ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBP10_MOUSE RBP10_MOUSE]] May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function.<ref>PMID:18347012</ref> <ref>PMID:19801445</ref> | + | [https://www.uniprot.org/uniprot/RBP10_MOUSE RBP10_MOUSE] May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function.<ref>PMID:18347012</ref> <ref>PMID:19801445</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Hong, S K]] | + | [[Category: Hong SK]] |
| - | [[Category: Kim, E E]] | + | [[Category: Kim EE]] |
| - | [[Category: Kim, K H]] | + | [[Category: Kim K-H]] |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Ran-binding protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
RBP10_MOUSE May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function.[1] [2]
Publication Abstract from PubMed
RanBPM and RanBP10 are non-canonical members of the Ran binding protein family that lack the Ran binding domain and do not associate with Ran GTPase in vivo. Rather, they have been shown to be scaffolding proteins that are important for a variety of cellular processes, and both of these proteins contain a SPRY domain, which has been implicated in mediating protein-protein interactions with a variety of targets including the DEAD-box containing ATP-dependent RNA helicase (DDX-4). In this study, we have determined the crystal structures of the SPIa and the ryanodine receptor domain and of approximately 70 upstream residues (immediate upstream to SPRY motif) of both RanBPM and RanBP10. They are almost identical, composed of a beta-sandwich fold with a set of two helices on each side located at the edge of the sheets. A unique shallow binding surface is formed by highly conserved loops on the surface of the beta-sheet with two aspartates on one end, a positive patch on the opposite end, and a tryptophan lining at the bottom of the surface. The 20-mer peptide (residues 228-247) of human DDX-4, an ATP-dependent RNA helicase known to regulate germ cell development, binds to this surface with a KD of ~13muM. The crystal structure of the peptide complex and the mutagenesis studies elucidate how RanBPM can recognize its interaction partners to function in gametogenesis.
Structural Basis for the Interaction between the IUS-SPRY Domain of RanBPM and DDX-4 in Germ Cell Development.,Hong SK, Kim KH, Song EJ, Kim EE J Mol Biol. 2016 Oct 23;428(21):4330-4344. doi: 10.1016/j.jmb.2016.09.004. Epub, 2016 Sep 10. PMID:27622290[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schulze H, Dose M, Korpal M, Meyer I, Italiano JE Jr, Shivdasani RA. RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules. J Biol Chem. 2008 May 16;283(20):14109-19. doi: 10.1074/jbc.M709397200. Epub 2008, Mar 17. PMID:18347012 doi:http://dx.doi.org/10.1074/jbc.M709397200
- ↑ Kunert S, Meyer I, Fleischhauer S, Wannack M, Fiedler J, Shivdasani RA, Schulze H. The microtubule modulator RanBP10 plays a critical role in regulation of platelet discoid shape and degranulation. Blood. 2009 Dec 24;114(27):5532-40. doi: 10.1182/blood-2009-04-216804. Epub 2009 , Oct 2. PMID:19801445 doi:http://dx.doi.org/10.1182/blood-2009-04-216804
- ↑ Hong SK, Kim KH, Song EJ, Kim EE. Structural Basis for the Interaction between the IUS-SPRY Domain of RanBPM and DDX-4 in Germ Cell Development. J Mol Biol. 2016 Oct 23;428(21):4330-4344. doi: 10.1016/j.jmb.2016.09.004. Epub, 2016 Sep 10. PMID:27622290 doi:http://dx.doi.org/10.1016/j.jmb.2016.09.004
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