1u9f

Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)

spinqualitylabelsall models 1u9f, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1u9f is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: ACE, TA4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gcn4 3D Structures Gnc4 3D Structures

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