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2y8g

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Revision as of 12:25, 27 April 2022

Structure of the Ran-binding domain from human RanBP3 (E352A-R353V double mutant)

Structural highlights

2y8g is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2y8f, 2crf
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RANB3_HUMAN] Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Proteins bearing a leucine-rich nuclear export signal (NES) are exported from the nucleus by the transport factor CRM1, which forms a cooperative ternary complex with the NES-bearing cargo and with the small GTPase Ran. CRM1-mediated export is regulated by RanBP3, a Ran-interacting nuclear protein. Unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, RanBP3 acts as a CRM1 cofactor, enhancing NES export by stabilizing the export complex in the nucleus. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. Here we report the crystal structure of the Ran-binding domain (RBD) from RanBP3 and compare it to RBD structures from RanBP1 and RanBP2 in complex with Ran and CRM1. Differences among these structures suggest why RanBP3 binds Ran with unusually low affinity, how RanBP3 modulates the cargo selectivity of CRM1, and why RanBP3 promotes assembly rather than disassembly of the export complex. The comparison of RBD structures thus provides an insight into the functional diversity of Ran-binding proteins.

Insights into the Function of the CRM1 Cofactor RanBP3 from the Structure of Its Ran-Binding Domain.,Langer K, Dian C, Rybin V, Muller CW, Petosa C PLoS One. 2011 Feb 25;6(2):e17011. PMID:21364925^[6]

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

References

↑ Mueller L, Cordes VC, Bischoff FR, Ponstingl H. Human RanBP3, a group of nuclear RanGTP binding proteins. FEBS Lett. 1998 May 15;427(3):330-6. PMID:9637251
↑ Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001 Oct;2(10):926-32. Epub 2001 Sep 24. PMID:11571268 doi:http://dx.doi.org/10.1093/embo-reports/kve200
↑ Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001 Jun 25;153(7):1391-402. PMID:11425870
↑ Nemergut ME, Lindsay ME, Brownawell AM, Macara IG. Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. J Biol Chem. 2002 May 17;277(20):17385-8. Epub 2002 Apr 3. PMID:11932251 doi:http://dx.doi.org/10.1074/jbc.C100620200
↑ Dai F, Lin X, Chang C, Feng XH. Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling. Dev Cell. 2009 Mar;16(3):345-57. doi: 10.1016/j.devcel.2009.01.022. PMID:19289081 doi:10.1016/j.devcel.2009.01.022
↑ Langer K, Dian C, Rybin V, Muller CW, Petosa C. Insights into the Function of the CRM1 Cofactor RanBP3 from the Structure of Its Ran-Binding Domain. PLoS One. 2011 Feb 25;6(2):e17011. PMID:21364925 doi:10.1371/journal.pone.0017011

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/2y8g"

@@ Line 3: / Line 3: @@
 <StructureSection load='2y8g' size='340' side='right'caption='[[2y8g]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y8g]] is a 2 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=2Y8G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Y8G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y8g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y8G FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y8f|2y8f]], [[2crf|2crf]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y8f|2y8f]], [[2crf|2crf]]</div></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=2y8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y8g OCA], [http://pdbe.org/2y8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y8g RCSB], [http://www.ebi.ac.uk/pdbsum/2y8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y8g ProSAT]</span></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=2y8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y8g OCA], [https://pdbe.org/2y8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y8g RCSB], [https://www.ebi.ac.uk/pdbsum/2y8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y8g ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RANB3_HUMAN RANB3_HUMAN]] Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.<ref>PMID:9637251</ref> <ref>PMID:11571268</ref> <ref>PMID:11425870</ref> <ref>PMID:11932251</ref> <ref>PMID:19289081</ref>
+[[https://www.uniprot.org/uniprot/RANB3_HUMAN RANB3_HUMAN]] Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export.<ref>PMID:9637251</ref> <ref>PMID:11571268</ref> <ref>PMID:11425870</ref> <ref>PMID:11932251</ref> <ref>PMID:19289081</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2y8g

From Proteopedia

Revision as of 12:25, 27 April 2022

Structure of the Ran-binding domain from human RanBP3 (E352A-R353V double mutant)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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