7q66
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7q66]] is a 22 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=7Q66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q66 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7q66]] is a 22 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=7Q66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q66 FirstGlance]. <br> | ||
| - | </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=7q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q66 OCA], [https://pdbe.org/7q66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q66 RCSB], [https://www.ebi.ac.uk/pdbsum/7q66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q66 ProSAT]</span></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]] 2.79Å</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=7q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q66 OCA], [https://pdbe.org/7q66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q66 RCSB], [https://www.ebi.ac.uk/pdbsum/7q66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q66 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient beta-structure and a stable preformed alpha-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG-FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities. | Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient beta-structure and a stable preformed alpha-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG-FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities. | ||
| - | Molecular interactions of FG nucleoporin repeats at high resolution.,Ibanez de Opakua A, Geraets JA, Frieg B, Dienemann C, Savastano A, Rankovic M, Cima-Omori MS, Schroder GF, Zweckstetter M Nat Chem. 2022 Nov;14(11):1278-1285. doi: 10.1038/s41557-022-01035-7. Epub 2022, Sep 22. PMID:36138110<ref>PMID:36138110</ref> | + | Molecular interactions of FG nucleoporin repeats at high resolution.,Ibanez de Opakua A, Geraets JA, Frieg B, Dienemann C, Savastano A, Rankovic M, Cima-Omori MS, Schroder GF, Zweckstetter M Nat Chem. 2022 Nov;14(11):1278-1285. doi: 10.1038/s41557-022-01035-7. Epub 2022 , Sep 22. PMID:36138110<ref>PMID:36138110</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 7q66" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7q66" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Nucleoporin 3D structures|Nucleoporin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Cryo-em structure of the Nup98 fibril polymorph 3
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