1llm: Difference between revisions

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

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

caption="1llm, resolution 1.50Å" />

'''Crystal Structure of a Zif23-GCN4 Chimera Bound to DNA'''<br />

==Overview==

Proteins that employ dimerization domains to bind cooperatively to DNA, have a number of potential advantages over monomers with regards to gene, regulation. Using a combination of structure-based design and phage, display, a dimeric Cys(2)His(2) zinc finger protein has been created that, binds cooperatively to DNA via an attached leucine zipper dimerization, domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A, resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA., This structure shows how phage display has annealed the DNA binding and, dimerization domains into a single functional unit. Moreover, this chimera, provides a potential platform for the creation heterodimeric zinc finger, proteins that can regulate a desired target gene through cooperative DNA, recognition.

Proteins that employ dimerization domains to bind cooperatively to DNA have a number of potential advantages over monomers with regards to gene regulation. Using a combination of structure-based design and phage display, a dimeric Cys(2)His(2) zinc finger protein has been created that binds cooperatively to DNA via an attached leucine zipper dimerization domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA. This structure shows how phage display has annealed the DNA binding and dimerization domains into a single functional unit. Moreover, this chimera provides a potential platform for the creation heterodimeric zinc finger proteins that can regulate a desired target gene through cooperative DNA recognition.

==About this Structure==

1LLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus_and_saccharomyces_cerevisiae Mus musculus and saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LLM OCA].

1LLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus_and_saccharomyces_cerevisiae Mus musculus and saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLM OCA].

==Reference==

Line 13:

[[Category: Mus musculus and saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Grant, R.A.]]

[[Category: Grant, R A.]]

[[Category: Pabo, C.O.]]

[[Category: Pabo, C O.]]

[[Category: Wolfe, S.A.]]

[[Category: Wolfe, S A.]]

[[Category: ZN]]

[[Category: dimerization]]

Line 24:

[[Category: zinc fingers]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:39:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:09 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1llm.jpg|left|200px]]<br /><applet load="1llm" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1llm.jpg|left|200px]]<br /><applet load="1llm" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1llm, resolution 1.50&Aring;" />
 '''Crystal Structure of a Zif23-GCN4 Chimera Bound to DNA'''<br />
 ==Overview==
-Proteins that employ dimerization domains to bind cooperatively to DNA, have a number of potential advantages over monomers with regards to gene, regulation. Using a combination of structure-based design and phage, display, a dimeric Cys(2)His(2) zinc finger protein has been created that, binds cooperatively to DNA via an attached leucine zipper dimerization, domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A, resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA., This structure shows how phage display has annealed the DNA binding and, dimerization domains into a single functional unit. Moreover, this chimera, provides a potential platform for the creation heterodimeric zinc finger, proteins that can regulate a desired target gene through cooperative DNA, recognition.
+Proteins that employ dimerization domains to bind cooperatively to DNA have a number of potential advantages over monomers with regards to gene regulation. Using a combination of structure-based design and phage display, a dimeric Cys(2)His(2) zinc finger protein has been created that binds cooperatively to DNA via an attached leucine zipper dimerization domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA. This structure shows how phage display has annealed the DNA binding and dimerization domains into a single functional unit. Moreover, this chimera provides a potential platform for the creation heterodimeric zinc finger proteins that can regulate a desired target gene through cooperative DNA recognition.
 ==About this Structure==
-LLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus_and_saccharomyces_cerevisiae Mus musculus and saccharomyces cerevisiae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LLM OCA].
+LLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus_and_saccharomyces_cerevisiae Mus musculus and saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLM OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus and saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Grant, R.A.]]
+[[Category: Grant, R A.]]
-[[Category: Pabo, C.O.]]
+[[Category: Pabo, C O.]]
-[[Category: Wolfe, S.A.]]
+[[Category: Wolfe, S A.]]
 [[Category: ZN]]
 [[Category: dimerization]]
@@ Line 24: / Line 24: @@
 [[Category: zinc fingers]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:39:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:09 2008''