1u9f: Difference between revisions
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[[ | ==Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)== | ||
<StructureSection load='1u9f' size='340' side='right' caption='[[1u9f]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1u9f]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U9F 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=TA4:(S)-2-[4-(AMINOMETHYL)-1H-1,2,3-TRIAZOL-1-YL]-4-METHYLPENTANOIC+ACID'>TA4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u9g|1u9g]], [[1u9h|1u9h]]</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=1u9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u9f RCSB], [http://www.ebi.ac.uk/pdbsum/1u9f PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this paper, we present 1,2,3-triazole epsilon2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known alpha-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the epsilon-residue. Crystal structures obtained for each peptide give insight into the chemical behavior and conformational preferences of the non-natural amino acid and show that the triazole ring can participate in the backbone hydrogen bonding of the alpha-helix as well as template an interhelical crossing between chains in the bundle. | |||
Heterocyclic peptide backbone modifications in an alpha-helical coiled coil.,Horne WS, Yadav MK, Stout CD, Ghadiri MR J Am Chem Soc. 2004 Dec 1;126(47):15366-7. PMID:15563148<ref>PMID:15563148</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Gcn4|Gcn4]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ghadiri, M R.]] | [[Category: Ghadiri, M R.]] | ||
[[Category: Horne, W S.]] | [[Category: Horne, W S.]] | ||
Revision as of 11:32, 8 October 2014
Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)
Structural highlights
Publication Abstract from PubMedIn this paper, we present 1,2,3-triazole epsilon2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known alpha-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the epsilon-residue. Crystal structures obtained for each peptide give insight into the chemical behavior and conformational preferences of the non-natural amino acid and show that the triazole ring can participate in the backbone hydrogen bonding of the alpha-helix as well as template an interhelical crossing between chains in the bundle. Heterocyclic peptide backbone modifications in an alpha-helical coiled coil.,Horne WS, Yadav MK, Stout CD, Ghadiri MR J Am Chem Soc. 2004 Dec 1;126(47):15366-7. PMID:15563148[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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