1zil
From Proteopedia
(New page: 200px<br /><applet load="1zil" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zil, resolution 2.25Å" /> '''GCN4-LEUCINE ZIPPER ...) |
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| - | [[Image:1zil.jpg|left|200px]]<br /><applet load="1zil" size=" | + | [[Image:1zil.jpg|left|200px]]<br /><applet load="1zil" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zil, resolution 2.25Å" /> | caption="1zil, resolution 2.25Å" /> | ||
'''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE DIMERIC STATE'''<br /> | '''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE DIMERIC STATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A conserved asparagine (Asn 16) buried in the interface of the GCN4 | + | A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gln and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn 16Lys mutant formed exclusively dimers. In contrast, Gln 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gln 16 side chain was accommodated by qualitatively different interactions in the dimer and trimer crystal structures. These findings demonstrate that the structural selectivity of polar residues results not only from the burial of polar atoms, but also depends on the complementarity of the side-chain stereochemistry with the surrounding structural environment. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1ZIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZIL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Junior, L | + | [[Category: Junior, L Gonzalez.]] |
| - | [[Category: Woolfson, D | + | [[Category: Woolfson, D N.]] |
[[Category: activator]] | [[Category: activator]] | ||
[[Category: amino-acid biosynthesis]] | [[Category: amino-acid biosynthesis]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:01 2008'' |
Revision as of 14:16, 21 February 2008
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GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE DIMERIC STATE
Overview
A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gln and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn 16Lys mutant formed exclusively dimers. In contrast, Gln 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gln 16 side chain was accommodated by qualitatively different interactions in the dimer and trimer crystal structures. These findings demonstrate that the structural selectivity of polar residues results not only from the burial of polar atoms, but also depends on the complementarity of the side-chain stereochemistry with the surrounding structural environment.
About this Structure
1ZIL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Buried polar residues and structural specificity in the GCN4 leucine zipper., Gonzalez L Jr, Woolfson DN, Alber T, Nat Struct Biol. 1996 Dec;3(12):1011-8. PMID:8946854
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