1piq
From Proteopedia
(New page: 200px<br /><applet load="1piq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1piq, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1piq.gif|left|200px]]<br /><applet load="1piq" size=" | + | [[Image:1piq.gif|left|200px]]<br /><applet load="1piq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1piq, resolution 1.80Å" /> | caption="1piq, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES'''<br /> | '''CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Coiled coils consist of two or more alpha-helices wrapped around each | + | 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== | ==About this Structure== | ||
| - | 1PIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CL and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1PIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIQ OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9837709 9837709] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9837709 9837709] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Eckert, D | + | [[Category: Eckert, D M.]] |
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
| - | [[Category: Malashkevich, V | + | [[Category: Malashkevich, V N.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: ion binding]] | [[Category: ion binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:10 2008'' |
Revision as of 12:29, 21 February 2008
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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 of sequence from [1] with and as ligands. 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
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