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2r2v

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{{STRUCTURE_2r2v| PDB=2r2v | SCENE= }}
{{STRUCTURE_2r2v| PDB=2r2v | SCENE= }}
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'''Sequence Determinants of the Topology of the Lac Repressor Tetrameric Coiled Coil'''
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===Sequence Determinants of the Topology of the Lac Repressor Tetrameric Coiled Coil===
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==Overview==
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Predictive understanding of how the folded, functional shape of a native protein is encoded in the linear sequence of its amino acid residues remains an unsolved challenge in modern structural biology. Antiparallel four-stranded coiled coils are relatively simple protein structures that embody a heptad sequence repeat and rich diversity for tertiary packing of alpha-helices. To explore specific sequence determinants of the lac repressor coiled-coil tetramerization domain, we have engineered a set of buried nonpolar side chains at the a-, d-, and e-positions into the hydrophobic interior of the dimeric GCN4 leucine zipper. Circular dichroism and equilibrium ultracentrifugation studies show that this core variant (GCN4-pAeLV) forms a stable tetrameric structure with a reversible and highly cooperative thermal unfolding transition. The X-ray crystal structure at 1.9 A reveals that GCN4-pAeLV is an antiparallel four-stranded coiled coil of the lac repressor type in which the a, d, and e side chains associate by means of combined knobs-against-knobs and knobs-into-holes packing with a characteristic interhelical offset of 0.25 heptad. Comparison of the side chain shape and packing in the antiparallel tetramers shows that the burial of alanine residues at the e positions between the neighboring helices of GCN4-pAeLV dictates both the antiparallel orientation and helix offset. This study fills in a gap in our knowledge of the determinants of structural specificity in antiparallel coiled coils and improves our understanding of how specific side chain packing forms the teritiary structure of a functional protein.
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{{ABSTRACT_PUBMED_18052214}}
==About this Structure==
==About this Structure==
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[[Category: De novo protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:48:40 2008''

Revision as of 23:48, 28 July 2008

Image:2r2v.png

Template:STRUCTURE 2r2v

Sequence Determinants of the Topology of the Lac Repressor Tetrameric Coiled Coil

Template:ABSTRACT PUBMED 18052214

About this Structure

2R2V is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Conformational specificity of the lac repressor coiled-coil tetramerization domain., Liu J, Zheng Q, Deng Y, Li Q, Kallenbach NR, Lu M, Biochemistry. 2007 Dec 25;46(51):14951-9. Epub 2007 Dec 4. PMID:18052214

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