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| | <SX load='5ijn' size='340' side='right' viewer='molstar' caption='[[5ijn]], [[Resolution|resolution]] 21.40Å' scene=''> | | <SX load='5ijn' size='340' side='right' viewer='molstar' caption='[[5ijn]], [[Resolution|resolution]] 21.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ijn]] is a 26 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=5IJN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ijn]] is a 26 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=5IJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IJN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUP62 ([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">Electron Microscopy, [[Resolution|Resolution]] 21.4Å</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=5ijn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ijn OCA], [http://pdbe.org/5ijn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ijn RCSB], [http://www.ebi.ac.uk/pdbsum/5ijn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ijn 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=5ijn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ijn OCA], [https://pdbe.org/5ijn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ijn RCSB], [https://www.ebi.ac.uk/pdbsum/5ijn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ijn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/NUP62_HUMAN NUP62_HUMAN]] Familial infantile bilateral striatal necrosis. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/NU155_HUMAN NU155_HUMAN]] Familial atrial fibrillation. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/NU155_HUMAN NU155_HUMAN] Familial atrial fibrillation. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NUP62_HUMAN NUP62_HUMAN]] Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex. [[http://www.uniprot.org/uniprot/NUP54_HUMAN NUP54_HUMAN]] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. [[http://www.uniprot.org/uniprot/NU155_HUMAN NU155_HUMAN]] Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.[UniProtKB:Q99P88] [[http://www.uniprot.org/uniprot/NU205_HUMAN NU205_HUMAN]] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC.<ref>PMID:15229283</ref> [[http://www.uniprot.org/uniprot/NUP93_HUMAN NUP93_HUMAN]] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC.<ref>PMID:15229283</ref> <ref>PMID:15703211</ref> [[http://www.uniprot.org/uniprot/NUP58_HUMAN NUP58_HUMAN]] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. | + | [https://www.uniprot.org/uniprot/NU155_HUMAN NU155_HUMAN] Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.[UniProtKB:Q99P88] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Appen, A von]]
| + | [[Category: Beck M]] |
| - | [[Category: Beck, M]] | + | [[Category: Kosinski J]] |
| - | [[Category: Kosinski, J]] | + | [[Category: Mosalaganti S]] |
| - | [[Category: Mosalaganti, S]] | + | [[Category: Von Appen A]] |
| - | [[Category: Nuclear pore complex]] | + | |
| - | [[Category: Nucleocytoplasmic transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Disease
NU155_HUMAN Familial atrial fibrillation. The disease is caused by mutations affecting the gene represented in this entry.
Function
NU155_HUMAN Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.[UniProtKB:Q99P88]
Publication Abstract from PubMed
Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these nucleoporins assemble into the NPC scaffold imposes a formidable challenge. Recently, it has been shown how the Y complex, a prominent NPC module, forms the outer rings of the nuclear pore. However, the organization of the inner ring has remained unknown until now. We used molecular modeling combined with cross-linking mass spectrometry and cryo-electron tomography to obtain a composite structure of the inner ring. This architectural map explains the vast majority of the electron density of the scaffold. We conclude that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar.
Molecular architecture of the inner ring scaffold of the human nuclear pore complex.,Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M Science. 2016 Apr 15;352(6283):363-5. doi: 10.1126/science.aaf0643. PMID:27081072[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M. Molecular architecture of the inner ring scaffold of the human nuclear pore complex. Science. 2016 Apr 15;352(6283):363-5. doi: 10.1126/science.aaf0643. PMID:27081072 doi:http://dx.doi.org/10.1126/science.aaf0643
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