1vrz

Helix turn helix motif

spinqualitylabelsall models 1vrz, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vrz is a 1 chain structure. This structure supersedes the now removed PDB entry 1q4f. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.05Å Ligands: 23F, ACE, ACT, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed De novo design of supersecondary structures is expected to provide useful molecular frameworks for the incorporation of functional sites as in proteins. A 21 residue long, dehydrophenylalanine-containing peptide has been de novo designed and its crystal structure determined. The apolar peptide folds into a helical hairpin supersecondary structure with two right-handed helices, connected by a tetraglycine linker. The helices of the hairpin interact with each other through a combination of C-H.O and N-H.O hydrogen bonds. The folding of the apolar peptide has been realized without the help of either metal ions or disulphide bonds. A remarkable feature of the peptide is the unanticipated occurrence of an anion binding motif in the linker region, strikingly similar in conformation and function to the "nest" motif seen in several proteins. The observation supports the view for the possible emergence of rudimentary functions over short sequence stretches in the early peptides under prebiotic conditions. De novo design and characterization of a helical hairpin eicosapeptide; emergence of an anion receptor in the linker region.,Rudresh, Ramakumar S, Ramagopal UA, Inai Y, Goel S, Sahal D, Chauhan VS Structure. 2004 Mar;12(3):389-96. PMID:15016355 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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