1vrz
From Proteopedia
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Helix turn helix motif
Overview
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.
About this Structure
1VRZ is a Protein complex structure of sequences from [1] with ACT, ACE and NH2 as ligands. This structure superseeds the now removed PDB entry 1Q4F. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sat Nov 24 23:08:26 2007
Categories: Protein complex | Inai, Y. | Ramagopal, U.A. | Ramakumar, S. | Rudresh | Sahal, D. | ACE | ACT | NH2 | Helix-turn-helix motif | Hth
