3f86: Difference between revisions
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[[ | ==An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quaternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions== | ||
<StructureSection load='3f86' size='340' side='right' caption='[[3f86]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3f86]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F86 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=B3L:(3S)-3-AMINO-5-METHYLHEXANOIC+ACID'>B3L</scene>, <scene name='pdbligand=B3M:(3R)-3-AMINO-5-(METHYLSULFANYL)PENTANOIC+ACID'>B3M</scene>, <scene name='pdbligand=BIL:(3R,4S)-3-AMINO-4-METHYLHEXANOIC+ACID'>BIL</scene>, <scene name='pdbligand=HMR:BETA-HOMOARGININE'>HMR</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oxk|2oxk]], [[2oxj|2oxj]], [[1gcl|1gcl]], [[2zta|2zta]]</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=3f86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f86 RCSB], [http://www.ebi.ac.uk/pdbsum/3f86 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Helix bundles are among the most widely studied tertiary and quaternary structural motifs in proteins. Here we present the crystal structure of an alpha/beta-peptide foldamer that adopts a tetrameric helix-bundle quaternary structure with a hydrophobic core composed solely of beta-amino acids. The structure displays features that are unprecedented among all known helix bundles composed of either alpha-peptides or peptidic foldamers. The tetramer is characterized by an asymmetry of interaction between neighboring helices, and the side-chain packing within the hydrophobic core differs fundamentally from the knobs-into-holes arrangement typical of most helix bundles. | |||
An alpha/beta-Peptide Helix Bundle with a Pure beta(3)-Amino Acid Core and a Distinctive Quaternary Structure.,Giuliano MW, Horne WS, Gellman SH J Am Chem Soc. 2009 Jul 6. PMID:19580264<ref>PMID:19580264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gellman, S H]] | |||
== | [[Category: Giuliano, M W]] | ||
< | [[Category: Horne, W S]] | ||
[[Category: Gellman, S H | |||
[[Category: Giuliano, M W | |||
[[Category: Horne, W S | |||
[[Category: Alpha/beta-peptide]] | [[Category: Alpha/beta-peptide]] | ||
[[Category: Foldamer]] | [[Category: Foldamer]] | ||
Revision as of 08:33, 26 November 2014
An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quaternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions
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