View source for 9jhi


==Cryo-em structure of beta-LG fibril==
<StructureSection load='9jhi' size='340' side='right'caption='[[9jhi]], [[Resolution|resolution]] 3.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jhi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JHI 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]] 3.73&#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=9jhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jhi OCA], [https://pdbe.org/9jhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jhi RCSB], [https://www.ebi.ac.uk/pdbsum/9jhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jhi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
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== Publication Abstract from PubMed ==
The beta-lactoglobulin (beta-LG) protein, sourced from dietary products, is notable for forming amyloid fibrils, which are increasingly recognized as valuable protein-based nanomaterials due to their superior cytocompatibility, chemical resilience, and mechanical characteristics. However, the precise atomic details of beta-LG's fibril assembly are not understood. In this study, we utilized cryo-electron microscopy to elucidate the composition and architecture of beta-LG fibrils. We discovered that the beta-LG fibril was rapidly assembled after a short time incubation. Remarkably, these fibril cores were composed of the first 32 residues, forming four beta-strands that adopted a serpentine arrangement into a single protofilament. This protofilament core's stability was reinforced by hydrophobic interactions. Two identical protofilaments then align to form four distinct structural polymorphs through unique interfacial configurations, which were stabilized by hydrophilic interactions, hydrogen bonding, and electrostatic forces. Our findings provide a structural framework for understanding beta-LG fibril formation and pave the way for designing innovative beta-LG-based nanomaterials.

beta-Lactoglobulin Forms a Conserved Fibril Core That Assembles into Diverse Fibril Polymorphs.,Xu Y, Li D, Zhang Y, Zhao Q, Sun B, Liu C, Li D, Dai B Nano Lett. 2025 Mar 5;25(9):3653-3661. doi: 10.1021/acs.nanolett.5c00137. Epub , 2025 Feb 24. PMID:39992798<ref>PMID:39992798</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Liu C]]
[[Category: Xu YY]]