View source for 6d02


==Cross-alpha Amyloid-like Structure alphaAmL, 2nd form==
<StructureSection load='6d02' size='340' side='right'caption='[[6d02]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6d02]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D02 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6d02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d02 OCA], [https://pdbe.org/6d02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d02 RCSB], [https://www.ebi.ac.uk/pdbsum/6d02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d02 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Amyloids adopt 'cross-beta' structures composed of long, twisted fibrils with beta-strands running perpendicular to the fibril axis. Recently, a toxic peptide was proposed to form amyloid-like cross-alpha structures in solution, with a planar bilayer-like assembly observed in the crystal structure. Here we crystallographically characterize designed peptides that assemble into spiraling cross-alpha amyloid-like structures, which resemble twisted beta-amyloid fibrils. The peptides form helical dimers, stabilized by packing of small and apolar residues, and the dimers further assemble into cross-alpha amyloid-like fibrils with superhelical pitches ranging from 170 A to 200 A. When a small residue that appeared critical for packing was converted to leucine, it resulted in structural rearrangement to a helical polymer. Fluorescently tagged versions of the designed peptides form puncta in mammalian cells, which recover from photobleaching with markedly different kinetics. These structural folds could be potentially useful for directing in vivo protein assemblies with predetermined spacing and stabilities.

Designed peptides that assemble into cross-alpha amyloid-like structures.,Zhang SQ, Huang H, Yang J, Kratochvil HT, Lolicato M, Liu Y, Shu X, Liu L, DeGrado WF Nat Chem Biol. 2018 Jul 30. pii: 10.1038/s41589-018-0105-5. doi:, 10.1038/s41589-018-0105-5. PMID:30061717<ref>PMID:30061717</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6d02" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Degrado WF]]
[[Category: Liu L]]
[[Category: Zhang S-Q]]