2zta
From Proteopedia
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X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL
Overview
The x-ray crystal structure of a peptide corresponding to the leucine, zipper of the yeast transcriptional activator GCN4 has been determined at, 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled, coil of alpha helices packed as in the "knobs-into-holes" model proposed, by Crick in 1953. Contacts between the helices include ion pairs and an, extensive hydrophobic interface that contains a distinctive hydrogen bond., The conserved leucines, like the residues in the alternate hydrophobic, repeat, make side-to-side interactions (as in a handshake) in every other, layer of the dimer interface. The crystal structure of the GCN4 leucine, zipper suggests a key role for the leucine repeat, but also shows how, other features of the coiled coil contribute to dimer formation.
About this Structure
2ZTA is a Single protein structure of sequence from Saccharomyces cerevisiae with ACE as ligand. The following page contains interesting information on the relation of 2ZTA with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil., O'Shea EK, Klemm JD, Kim PS, Alber T, Science. 1991 Oct 25;254(5031):539-44. PMID:1948029
Page seeded by OCA on Sun Nov 18 09:10:02 2007
