1zta

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zta OCA], [http://www.ebi.ac.uk/pdbsum/1zta PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zta RCSB]</span>
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'''THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE'''
'''THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE'''
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[[Category: Pastore, A.]]
[[Category: Pastore, A.]]
[[Category: Saudek, V.]]
[[Category: Saudek, V.]]
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[[Category: dna-binding motif]]
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[[Category: Dna-binding motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:02:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:41:23 2008''
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Revision as of 15:02, 3 May 2008

Template:STRUCTURE 1zta

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 Page seeded by OCA on Sat May 3 18:02:39 2008

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