7qdk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='7qdk' size='340' side='right'caption='[[7qdk]], [[Resolution|resolution]] 1.41Å' scene=''> | <StructureSection load='7qdk' size='340' side='right'caption='[[7qdk]], [[Resolution|resolution]] 1.41Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7qdk]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QDK FirstGlance]. <br> | <table><tr><td colspan='2'>[[7qdk]] is a 3 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=7QDK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QDK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4BF:4-BROMO-L-PHENYLALANINE'>4BF</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=7qdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qdk OCA], [https://pdbe.org/7qdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qdk RCSB], [https://www.ebi.ac.uk/pdbsum/7qdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qdk ProSAT]</span></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=7qdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qdk OCA], [https://pdbe.org/7qdk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qdk RCSB], [https://www.ebi.ac.uk/pdbsum/7qdk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qdk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| Line 22: | Line 21: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Kumar P]] | ||
[[Category: | [[Category: Paterson NG]] | ||
[[Category: | [[Category: Woolfson DN]] | ||
Latest revision as of 07:41, 8 September 2022
A trimeric de novo coiled-coil assembly: CC-TypeN-LaLdA trimeric de novo coiled-coil assembly: CC-TypeN-LaLd
Structural highlights
Publication Abstract from PubMedThe alpha-helix is pre-eminent in structural biology(1) and widely exploited in protein folding(2), design(3) and engineering(4). Although other helical peptide conformations do exist near to the alpha-helical region of conformational space-namely, 310-helices and pi-helices(5)-these occur much less frequently in protein structures. Less favourable internal energies and reduced tendencies to pack into higher-order structures mean that 310-helices rarely exceed six residues in length in natural proteins, and that they tend not to form normal supersecondary, tertiary or quaternary interactions. Here we show that despite their absence in nature, synthetic peptide assemblies can be built from 310-helices. We report the rational design, solution-phase characterization and an X-ray crystal structure for water-soluble bundles of 310-helices with consolidated hydrophobic cores. The design uses six-residue repeats informed by analysing 310-helical conformations in known protein structures, and incorporates alpha-aminoisobutyric acid residues. Design iterations reveal a tipping point between alpha-helical and 310-helical folding, and identify features required for stabilizing assemblies of 310-helices. This work provides principles and rules to open opportunities for designing into this hitherto unexplored region of protein-structure space. De novo design of discrete, stable 310-helix peptide assemblies.,Kumar P, Paterson NG, Clayden J, Woolfson DN Nature. 2022 Jun 22. pii: 10.1038/s41586-022-04868-x. doi:, 10.1038/s41586-022-04868-x. PMID:35732733[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||