7zj2: Difference between revisions

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-'''Unreleased structure'''
-The entry 7zj2 is ON HOLD  until Paper Publication
+==Amyloid fibril (in vitro) from full-length hnRNPA1 protein==
+<StructureSection load='7zj2' size='340' side='right'caption='[[7zj2]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7zj2]] is a 12 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=7ZJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZJ2 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.32&#8491;</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=7zj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zj2 OCA], [https://pdbe.org/7zj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zj2 RCSB], [https://www.ebi.ac.uk/pdbsum/7zj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zj2 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN] Amyotrophic lateral sclerosis;Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>   The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ROA1_HUMAN ROA1_HUMAN] Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection. May play a role in HCV RNA replication.<ref>PMID:17229681</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) is a multifunctional RNA-binding protein that is associated with neurodegenerative diseases, such as amyotrophic lateral sclerosis and multisystem proteinopathy. In this study, we have used cryo-electron microscopy to investigate the three-dimensional structure of amyloid fibrils from full-length hnRNPA1 protein. We find that the fibril core is formed by a 45-residue segment of the prion-like low-complexity domain of the protein, whereas the remaining parts of the protein (275 residues) form a fuzzy coat around the fibril core. The fibril consists of two fibril protein stacks that are arranged into a pseudo-2(1) screw symmetry. The ordered core harbors several of the positions that are known to be affected by disease-associated mutations, but does not encompass the most aggregation-prone segments of the protein. These data indicate that the structures of amyloid fibrils from full-length proteins may be more complex than anticipated by current theories on protein misfolding.
-Authors:
+Cryo-EM Structure of the Full-length hnRNPA1 Amyloid Fibril.,Sharma K, Banerjee S, Savran D, Rajes C, Wiese S, Girdhar A, Schwierz N, Lee C, Shorter J, Schmidt M, Guo L, Fandrich M J Mol Biol. 2023 Jul 20;435(18):168211. doi: 10.1016/j.jmb.2023.168211. PMID:37481159<ref>PMID:37481159</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7zj2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Banerjee S]]
+[[Category: Faendrich M]]
+[[Category: Schmidt M]]
+[[Category: Sharma K]]