2crf: Difference between revisions

Latest revision as of 11:29, 22 May 2024

Solution structure of the Ran_BP1 domain of RAN-binding protein-3

Structural highlights

2crf is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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:https://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:https://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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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:https://dx.doi.org/10.1093/embo-reports/kve200

[3] 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

[4] 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:https://dx.doi.org/10.1074/jbc.C100620200

[5] 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

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
 ==Solution structure of the Ran_BP1 domain of RAN-binding protein-3==
-<StructureSection load='2crf' size='340' side='right' caption='[[2crf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2crf' size='340' side='right'caption='[[2crf]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2crf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CRF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2crf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CRF FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RANBP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2crf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2crf OCA], [http://pdbe.org/2crf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2crf RCSB], [http://www.ebi.ac.uk/pdbsum/2crf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2crf ProSAT], [http://www.topsan.org/Proteins/RSGI/2crf TOPSAN]</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=2crf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2crf OCA], [https://pdbe.org/2crf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2crf RCSB], [https://www.ebi.ac.uk/pdbsum/2crf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2crf ProSAT], [https://www.topsan.org/Proteins/RSGI/2crf TOPSAN]</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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Hayashi, F]]
+[[Category: Large Structures]]
-[[Category: Nagashima, T]]
+[[Category: Hayashi F]]
-[[Category: Structural genomic]]
+[[Category: Nagashima T]]
-[[Category: Yokoyama, S]]
+[[Category: Yokoyama S]]
-[[Category: Zhang, H P]]
+[[Category: Zhang HP]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Ran-binding protein 3]]
-[[Category: Ran_bp1 domain]]
-[[Category: Ranbp3]]
-[[Category: Rsgi]]
-[[Category: Transport protein]]

2crf: Difference between revisions

Latest revision as of 11:29, 22 May 2024

Solution structure of the Ran_BP1 domain of RAN-binding protein-3

Structural highlights

Function

Evolutionary Conservation

References

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