1zik: Difference between revisions

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[[Image:1zik.gif|left|200px]]<br /><applet load="1zik" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1zik.gif|left|200px]]<br /><applet load="1zik" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1zik, resolution 1.8Å" />

'''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16LYS IN THE DIMERIC STATE'''<br />

==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.

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==

1ZIK 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ZIK OCA].

1ZIK 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=1ZIK OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Alber, T.]]

[[Category: Junior, L.Gonzalez.]]

[[Category: Junior, L Gonzalez.]]

[[Category: Woolfson, D.N.]]

[[Category: Woolfson, D N.]]

[[Category: activator]]

[[Category: amino-acid biosynthesis]]

Line 24:

[[Category: transcription regulation]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1zik.gif|left|200px]]<br /><applet load="1zik" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zik.gif|left|200px]]<br /><applet load="1zik" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zik, resolution 1.8&Aring;" />
 '''GCN4-LEUCINE ZIPPER CORE MUTANT ASN16LYS IN THE DIMERIC STATE'''<br />
 ==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.
+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==
-ZIK 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZIK OCA].
+ZIK 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=1ZIK OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Alber, T.]]
-[[Category: Junior, L.Gonzalez.]]
+[[Category: Junior, L Gonzalez.]]
-[[Category: Woolfson, D.N.]]
+[[Category: Woolfson, D N.]]
 [[Category: activator]]
 [[Category: amino-acid biosynthesis]]
@@ Line 24: / Line 24: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:28:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:55 2008''