5eon: Difference between revisions
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==Crystal structure of a de novo antiparallel coiled-coil hexamer - ACC-Hex== | |||
<StructureSection load='5eon' size='340' side='right' caption='[[5eon]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5eon]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EON FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=LYN:2,6-DIAMINO-HEXANOIC+ACID+AMIDE'>LYN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eon OCA], [http://pdbe.org/5eon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eon RCSB], [http://www.ebi.ac.uk/pdbsum/5eon PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The self-assembly of peptides and proteins into higher-ordered structures is encoded in the amino acid sequence of each peptide or protein. Understanding the relationship among the amino acid sequence, the assembly dynamics, and the structure of well-defined peptide oligomers expands the synthetic toolbox for these structures. Here, we present the X-ray crystallographic structure and solution behavior of de novo peptides that form antiparallel coiled-coil hexamers (ACC-Hex) by an interaction motif neither found in nature nor predicted by existing peptide design software. The 1.70 A X-ray crystallographic structure of peptide 1a shows six alpha-helices associating in an antiparallel arrangement around a central axis comprising hydrophobic and aromatic residues. Size-exclusion chromatography studies suggest that peptides 1 form stable oligomers in solution, and circular dichroism experiments show that peptides 1 are stable to relatively high temperatures. Small-angle X-ray scattering studies of the solution behavior of peptide 1a indicate an equilibrium of dimers, hexamers, and larger aggregates in solution. The structures presented here represent a new motif of biomolecular self-assembly not previously observed for de novo peptides and suggest supramolecular design principles for material scaffolds based on coiled-coil motifs containing aromatic residues. | |||
X-ray Crystallographic Structure and Solution Behavior of an Antiparallel Coiled-Coil Hexamer Formed by de Novo Peptides.,Spencer RK, Hochbaum AI Biochemistry. 2016 May 27. PMID:27192036<ref>PMID:27192036</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Spencer, R | <div class="pdbe-citations 5eon" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hochbaum, A I]] | |||
[[Category: Spencer, R K]] | |||
[[Category: Antiparallel]] | |||
[[Category: Coiled-coil]] | |||
[[Category: De novo protein]] | |||
[[Category: Hexamer]] | |||
Revision as of 08:29, 1 June 2016
Crystal structure of a de novo antiparallel coiled-coil hexamer - ACC-Hex
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