3c3f: Difference between revisions
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[[ | ==alpha/beta-Peptide helix bundles: The GCN4-pLI side chain sequence on an (alpha-alpha-alpha-beta) backbone== | ||
<StructureSection load='3c3f' size='340' side='right' caption='[[3c3f]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3c3f]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C3F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C3F FirstGlance]. <br> | |||
</td></tr><tr><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=B3D:3-AMINOPENTANEDIOIC+ACID'>B3D</scene>, <scene name='pdbligand=B3E:(3S)-3-AMINOHEXANEDIOIC+ACID'>B3E</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</scene>, <scene name='pdbligand=B3L:(3S)-3-AMINO-5-METHYLHEXANOIC+ACID'>B3L</scene>, <scene name='pdbligand=BAL:BETA-ALANINE'>BAL</scene>, <scene name='pdbligand=BIL:(3R,4S)-3-AMINO-4-METHYLHEXANOIC+ACID'>BIL</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gcl|1gcl]], [[1uo2|1uo2]], [[2oxk|2oxk]], [[3c3g|3c3g]], [[3c3h|3c3h]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c3f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c3f RCSB], [http://www.ebi.ac.uk/pdbsum/3c3f PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The extent to which polypeptide conformation depends on side-chain composition and sequence has been widely studied, but less is known about the importance of maintaining an alpha-amino acid backbone. Here, we examine a series of peptides with backbones that feature different repeating patterns of alpha- and beta-amino acid residues but an invariant side-chain sequence. In the pure alpha-backbone, this sequence corresponds to the previously studied peptide GCN4-pLI, which forms a very stable four-helix bundle quaternary structure. Physical characterization in solution and crystallographic structure determination show that a variety of alpha/beta-peptide backbones can adopt sequence-encoded quaternary structures similar to that of the alpha prototype. There is a loss in helix bundle stability upon beta-residue incorporation; however, stability of the quaternary structure is not a simple function of beta-residue content. We find that cyclically constrained beta-amino acid residues can stabilize the folds of alpha/beta-peptide GCN4-pLI analogues and restore quaternary structure formation to backbones that are predominantly unfolded in the absence of cyclic residues. Our results show a surprising degree of plasticity in terms of the backbone compositions that can manifest the structural information encoded in a sequence of amino acid side chains. These findings offer a framework for the design of nonnatural oligomers that mimic the structural and functional properties of proteins. | |||
Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly.,Horne WS, Price JL, Gellman SH Proc Natl Acad Sci U S A. 2008 Jul 8;105(27):9151-6. Epub 2008 Jun 27. PMID:18587049<ref>PMID:18587049</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: Gellman, S H.]] | ||
[[Category: Horne, W S.]] | [[Category: Horne, W S.]] | ||
Revision as of 06:48, 9 June 2014
alpha/beta-Peptide helix bundles: The GCN4-pLI side chain sequence on an (alpha-alpha-alpha-beta) backbone
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