1u9f
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1u9f |SIZE=350|CAPTION= <scene name='initialview01'>1u9f</scene>, resolution 2.20Å | |PDB= 1u9f |SIZE=350|CAPTION= <scene name='initialview01'>1u9f</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1u9g|1U9G]], [[1u9h|1U9H]] | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1u9f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u9f RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
[[Category: Yadav, M K.]] | [[Category: Yadav, M K.]] | ||
| - | [[Category: ACE]] | ||
[[Category: heterocycic backbone modification]] | [[Category: heterocycic backbone modification]] | ||
[[Category: tetrameric alpha-helical coiled coil]] | [[Category: tetrameric alpha-helical coiled coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:07:15 2008'' |
Revision as of 21:07, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1U9G, 1U9H
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)
Overview
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.
About this Structure
1U9F is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
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