1zta
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(New page: 200px<br /><applet load="1zta" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zta" /> '''THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER M...)
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Revision as of 05:31, 21 November 2007
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THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE
Overview
We report the complete structure determination of a 34 residue synthetic, peptide with the amino acid sequence of the dimerization domain (leucine, zipper) of GCN4. A high resolution structure in solution was obtained by, 1H-NMR studies and distance geometry calculations followed by restrained, energy minimization. A set of 20 final structures was obtained with an, average root mean square deviation of 1.3 A for the backbone atoms, (excluding the first and the last two residues). The structure contains an, uninterrupted helix. A comparison with a structure previously determined, for a larger peptide containing both the DNA-binding region (basic region), and the leucine-zipper motif shows the structural independence of the, leucine-zipper domain from the contiguous DNA binding region.
About this Structure
1ZTA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The solution structure of a leucine-zipper motif peptide., Saudek V, Pastore A, Morelli MA, Frank R, Gausepohl H, Gibson T, Protein Eng. 1991 Jun;4(5):519-29. PMID:1891459
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