5ji7

From Proteopedia

(Difference between revisions)

Revision as of 18:52, 20 September 2023

The Crystal Structure Of IUS-SPRY Domain From RanBPM/9

Structural highlights

5ji7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.51Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RANB9_HUMAN May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang D, Li Z, Messing EM, Wu G. Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM. J Biol Chem. 2002 Sep 27;277(39):36216-22. Epub 2002 Jul 29. PMID:12147692 doi:http://dx.doi.org/10.1074/jbc.M205111200
↑ Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS. RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor. J Biol Chem. 2002 Dec 13;277(50):48020-7. Epub 2002 Oct 1. PMID:12361945 doi:http://dx.doi.org/10.1074/jbc.M209741200
↑ Zou Y, Lim S, Lee K, Deng X, Friedman E. Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M. J Biol Chem. 2003 Dec 5;278(49):49573-81. Epub 2003 Sep 18. PMID:14500717 doi:http://dx.doi.org/10.1074/jbc.M307556200
↑ Denti S, Sirri A, Cheli A, Rogge L, Innamorati G, Putignano S, Fabbri M, Pardi R, Bianchi E. RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1. J Biol Chem. 2004 Mar 26;279(13):13027-34. Epub 2004 Jan 13. PMID:14722085 doi:http://dx.doi.org/10.1074/jbc.M313515200
↑ Menon RP, Gibson TJ, Pastore A. The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J Mol Biol. 2004 Oct 8;343(1):43-53. PMID:15381419 doi:http://dx.doi.org/10.1016/j.jmb.2004.08.024
↑ Kramer S, Ozaki T, Miyazaki K, Kato C, Hanamoto T, Nakagawara A. Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells. Oncogene. 2005 Jan 27;24(5):938-44. PMID:15558019 doi:http://dx.doi.org/1208257
↑ Harada N, Yokoyama T, Yamaji R, Nakano Y, Inui H. RanBP10 acts as a novel coactivator for the androgen receptor. Biochem Biophys Res Commun. 2008 Mar 28;368(1):121-5. doi:, 10.1016/j.bbrc.2008.01.072. Epub 2008 Jan 24. PMID:18222118 doi:http://dx.doi.org/10.1016/j.bbrc.2008.01.072
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ji7"

Categories: Homo sapiens | Large Structures | Hong SK | Kim EE | Kim K-H

@@ Line 3: / Line 3: @@
 <StructureSection load='5ji7' size='340' side='right'caption='[[5ji7]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ji7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JI7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ji7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JI7 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ji9|5ji9]], [[5jia|5jia]], [[5jiu|5jiu]]</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]] 1.51&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RANBP9, RANBPM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5ji7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji7 OCA], [https://pdbe.org/5ji7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ji7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ji7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji7 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=5ji7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji7 OCA], [http://pdbe.org/5ji7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ji7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ji7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RANB9_HUMAN RANB9_HUMAN]] May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity).<ref>PMID:12147692</ref> <ref>PMID:12361945</ref> <ref>PMID:14500717</ref> <ref>PMID:14722085</ref> <ref>PMID:15381419</ref> <ref>PMID:15558019</ref> <ref>PMID:18222118</ref>
+[https://www.uniprot.org/uniprot/RANB9_HUMAN RANB9_HUMAN] May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA (By similarity).<ref>PMID:12147692</ref> <ref>PMID:12361945</ref> <ref>PMID:14500717</ref> <ref>PMID:14722085</ref> <ref>PMID:15381419</ref> <ref>PMID:15558019</ref> <ref>PMID:18222118</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[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]]

5ji7

From Proteopedia

Revision as of 18:52, 20 September 2023

The Crystal Structure Of IUS-SPRY Domain From RanBPM/9

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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