1piq

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[[Image:1piq.gif|left|200px]]
[[Image:1piq.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1piq", creates the "Structure Box" on the page.
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{{STRUCTURE_1piq| PDB=1piq | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1piq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1piq OCA], [http://www.ebi.ac.uk/pdbsum/1piq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1piq RCSB]</span>
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'''CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES'''
'''CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES'''
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==About this Structure==
==About this Structure==
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1PIQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIQ OCA].
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1PIQ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIQ OCA].
==Reference==
==Reference==
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[[Category: Kim, P S.]]
[[Category: Kim, P S.]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
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[[Category: buried polar residue]]
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[[Category: Buried polar residue]]
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[[Category: coiled coil]]
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[[Category: Coiled coil]]
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[[Category: ion binding]]
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[[Category: Ion binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:07:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:10 2008''
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Revision as of 02:07, 3 May 2008

Template:STRUCTURE 1piq

CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES


Overview

Coiled coils consist of two or more alpha-helices wrapped around each other with a superhelical twist. The interfaces between helices of a coiled coil are formed by hydrophobic amino acid residues packed in a "knobs-into-holes" arrangement. Most naturally occurring coiled coils, however, also contain buried polar residues, as do the cores of the majority of naturally occurring globular proteins. Two common buried polar residues in both dimeric and trimeric coiled coils are asparagine and glutamine. In dimeric coiled coils, buried asparagine, but not glutamine, residues have been shown to confer specificity of oligomerization. We have placed a glutamine residue in the otherwise hydrophobic interior of a stable trimeric coiled coil, GCN4-pII, to study the effect of this buried polar residue in a trimeric coiled-coil environment. The resulting peptide, GCN4-pIQI, is a discrete, trimeric coiled coil with a lower stability than GCN4-pII. The crystal structure determined to 1.8 A shows that GCN4-pIQI is a trimeric coiled coil with a chloride ion coordinated by one buried glutamine residue from each monomer.

About this Structure

1PIQ is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues., Eckert DM, Malashkevich VN, Kim PS, J Mol Biol. 1998 Dec 11;284(4):859-65. PMID:9837709 Page seeded by OCA on Sat May 3 05:07:39 2008

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