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3f87

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[[Image:3f87.png|left|200px]]
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==An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quarternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions - higher symmetry crystal==
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<StructureSection load='3f87' size='340' side='right' caption='[[3f87]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3f87]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F87 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene><br>
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<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=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>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oxj|2oxj]], [[2oxk|2oxk]], [[1gcl|1gcl]], [[2zta|2zta]]</td></tr>
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<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=3f87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f87 RCSB], [http://www.ebi.ac.uk/pdbsum/3f87 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_3f87", creates the "Structure Box" on the page.
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{{STRUCTURE_3f87| PDB=3f87 | SCENE= }}
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===An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quarternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions - higher symmetry crystal===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_19580264}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 19580264 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_19580264}}
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==About this Structure==
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[[3f87]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F87 OCA].
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==Reference==
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<ref group="xtra">PMID:019580264</ref><references group="xtra"/>
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[[Category: Gellman, S H.]]
[[Category: Gellman, S H.]]
[[Category: Giuliano, M W.]]
[[Category: Giuliano, M W.]]

Revision as of 09:50, 21 May 2014

An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quarternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions - higher symmetry crystal

3f87, resolution 2.40Å

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