1gcl: Difference between revisions

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{{STRUCTURE_1gcl|  PDB=1gcl  |  SCENE=  }}  
{{STRUCTURE_1gcl|  PDB=1gcl  |  SCENE=  }}  


'''GCN4 LEUCINE ZIPPER CORE MUTANT P-LI'''
===GCN4 LEUCINE ZIPPER CORE MUTANT P-LI===




==Overview==
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Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.
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{{ABSTRACT_PUBMED_8248779}}


==About this Structure==
==About this Structure==
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[[Category: Zhang, T.]]
[[Category: Zhang, T.]]
[[Category: Hydrophobic core mutant]]
[[Category: Hydrophobic core mutant]]
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Revision as of 05:05, 1 July 2008

File:1gcl.png

Template:STRUCTURE 1gcl

GCN4 LEUCINE ZIPPER CORE MUTANT P-LIGCN4 LEUCINE ZIPPER CORE MUTANT P-LI

Template:ABSTRACT PUBMED 8248779

About this StructureAbout this Structure

1GCL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants., Harbury PB, Zhang T, Kim PS, Alber T, Science. 1993 Nov 26;262(5138):1401-7. PMID:8248779

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