View source for 9vnk


==Cryo-EM structure of hnRAC1-2,8beta fibril polymorph2==
<StructureSection load='9vnk' size='340' side='right'caption='[[9vnk]], [[Resolution|resolution]] 3.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vnk]] is a 54 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=9VNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VNK 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]] 3.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFE:(3S)-3-AMINO-3-PHENYLPROPANOIC+ACID'>SFE</scene></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=9vnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vnk OCA], [https://pdbe.org/9vnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vnk RCSB], [https://www.ebi.ac.uk/pdbsum/9vnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vnk ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The self-assembly of peptides into amyloid fibrils enables the design of functional biomaterials, yet the conformational constraints of alpha-peptides limit the attainable supramolecular diversity. Here, we introduce beta-amino acids, beta-phenylalanine (beta-Phe), and beta-homophenylalanine (beta-hPhe) into the reversible fibril-forming core sequence hnRAC1 to generate alpha/beta-peptide variants with distinct architectures and enhanced thermal stability. Cryo-EM reveals that beta-modified peptides assemble into polymorphic fibrils with cross-beta structures that differ markedly from each other and from native hnRAC1. Comparative structural analysis indicates that backbone extension by beta-residues increases subunit conformational heterogeneity, enabling tighter packing and formation of more thermostable fibrils. Examination of intra- and intermolecular contacts shows that enhanced pi-pi stacking, hydrophobic interactions, hydrogen bonds, and electrostatic interactions likely contribute to fibril stabilization. These results show that minimal backbone modifications can remodel amyloid architecture, offering a generalizable strategy for designing structurally diverse and robust peptide-based biomaterials.

Conformational Adaptability and Thermostability in alpha/beta-Peptide Fibrils Induced by beta-Amino Acid Substitution.,Li Y, Li D, Yao Y, Liu K, Zhao Q, Zhang Y, Xu Y, Li D, Sun B, Liu C, Dai B Nano Lett. 2025 Dec 20. doi: 10.1021/acs.nanolett.5c05223. PMID:41420871<ref>PMID:41420871</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vnk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dai B]]
[[Category: Li DN]]
[[Category: Li YS]]