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{{STRUCTURE_4bsn| PDB=4bsn | SCENE= }} | |||
===Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.1A=== | |||
{{ABSTRACT_PUBMED_23850454}} | |||
The | ==Function== | ||
[[http://www.uniprot.org/uniprot/XPO1_HUMAN XPO1_HUMAN]] Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.<ref>PMID:9323133</ref> <ref>PMID:9311922</ref> <ref>PMID:9837918</ref> <ref>PMID:14612415</ref> <ref>PMID:15574332</ref> <ref>PMID:20921223</ref> | |||
==About this Structure== | |||
[[4bsn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BSN OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:023850454</ref><references group="xtra"/><references/> | |||
[[Category: Homo sapiens]] | |||
[[Category: Bernaudat, F.]] | |||
[[Category: Dian, C.]] | |||
[[Category: Fornerod, M.]] | |||
[[Category: Langer, K.]] | |||
[[Category: Muller, C W.]] | |||
[[Category: Oliva, M F.]] | |||
[[Category: Petosa, C.]] | |||
[[Category: Schoehn, G.]] | |||
[[Category: Heat repeat protein]] | |||
[[Category: Importin-beta superfamily]] | |||
[[Category: Nucleocytoplasmic transport of protein and rnp cargo]] | |||
[[Category: Protein transport]] | |||
Revision as of 08:13, 1 August 2013
Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.1ACrystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.1A
Template:ABSTRACT PUBMED 23850454
FunctionFunction
[XPO1_HUMAN] Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.[1] [2] [3] [4] [5] [6]
About this StructureAbout this Structure
4bsn is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Dian C, Bernaudat F, Langer K, Oliva MF, Fornerod M, Schoehn G, Muller CW, Petosa C. Structure of a Truncation Mutant of the Nuclear Export Factor CRM1 Provides Insights into the Auto-Inhibitory Role of Its C-Terminal Helix. Structure. 2013 Jul 9. pii: S0969-2126(13)00202-5. doi:, 10.1016/j.str.2013.06.003. PMID:23850454 doi:10.1016/j.str.2013.06.003
- ↑ Fornerod M, Ohno M, Yoshida M, Mattaj IW. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 1997 Sep 19;90(6):1051-60. PMID:9323133
- ↑ Ossareh-Nazari B, Bachelerie F, Dargemont C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science. 1997 Oct 3;278(5335):141-4. PMID:9311922
- ↑ Askjaer P, Jensen TH, Nilsson J, Englmeier L, Kjems J. The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J Biol Chem. 1998 Dec 11;273(50):33414-22. PMID:9837918
- ↑ Hakata Y, Yamada M, Shida H. A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein. Mol Cell Biol. 2003 Dec;23(23):8751-61. PMID:14612415
- ↑ Boulon S, Verheggen C, Jady BE, Girard C, Pescia C, Paul C, Ospina JK, Kiss T, Matera AG, Bordonne R, Bertrand E. PHAX and CRM1 are required sequentially to transport U3 snoRNA to nucleoli. Mol Cell. 2004 Dec 3;16(5):777-87. PMID:15574332 doi:10.1016/j.molcel.2004.11.013
- ↑ Fei E, Ma X, Zhu C, Xue T, Yan J, Xu Y, Zhou J, Wang G. Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related protein, regulates synapsin I expression. J Biol Chem. 2010 Dec 3;285(49):38630-40. doi: 10.1074/jbc.M110.107912. Epub 2010, Oct 4. PMID:20921223 doi:10.1074/jbc.M110.107912