2zta: Difference between revisions

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[[Image:2zta.~~gif~~|left|200px]]

[[Image:2zta.png|left|200px]]

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~~==Overview==~~

The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.

==About this Structure==

2ZTA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 2ZTA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZTA OCA].

~~==Reference==~~

X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil., O'Shea EK, Klemm JD, Kim PS, Alber T, Science. 1991 Oct 25;254(5031):539-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1948029 1948029]

[[Category: Designer Proteins]]

[[Category: Saccharomyces cerevisiae]]

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[[Category: Shea, E K.O.]]

[[Category: Leucine zipper]]

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-[[Image:2zta.gif|left|200px]]
+[[Image:2zta.png|left|200px]]
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-==Overview==
+{{ABSTRACT_1948029}}
-The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
 ==About this Structure==
 ZTA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 2ZTA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZTA OCA].
-==Reference==
-X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil., O'Shea EK, Klemm JD, Kim PS, Alber T, Science. 1991 Oct 25;254(5031):539-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1948029 1948029]
 [[Category: Designer Proteins]]
 [[Category: Saccharomyces cerevisiae]]
@@ Line 28: / Line 24: @@
 [[Category: Shea, E K.O.]]
 [[Category: Leucine zipper]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:14:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:25:10 2008''