@article {47506,
	title = {Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril.},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {113},
	year = {2016},
	month = {2016 May 16},
	pages = {6200-5},
	abstract = {<p>Amyloid fibrils are proteinaceous aggregates associated with diseases in humans and animals. The fibrils are defined by intermolecular interactions between the fibril-forming polypeptide chains, but it has so far remained difficult to reveal the assembly of the peptide subunits in a full-scale fibril. Using electron cryomicroscopy (cryo-EM), we present a reconstruction of a fibril formed from the pathogenic core of an amyloidogenic immunoglobulin (Ig) light chain. The fibril density shows a lattice-like assembly of face-to-face packed peptide dimers that corresponds to the structure of steric zippers in peptide crystals. Interpretation of the density map with a molecular model enabled us to identify the intermolecular interactions between the peptides and rationalize the hierarchical structure of the fibril based on simple chemical principles.</p>
},
	issn = {1091-6490},
	doi = {10.1073/pnas.1522282113},
	author = {Schmidt, Andreas and Annamalai, Karthikeyan and Schmidt, Matthias and Grigorieff, Nikolaus and F{\"a}ndrich, Marcus}
}
