1vhi: Difference between revisions

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

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

caption="1vhi, resolution 2.5Å" />

'''EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607'''<br />

==Overview==

The crystal structure of the DNA-binding and dimerization domains of the, Epstein-Barr virus nuclear antigen 1 (EBNA1), which binds to and activates, DNA replication from the latent origin of replication in Epstein-Barr, virus, was solved at 2.5 A resolution. EBNA1 appears to bind DNA via two, independent regions termed the core and the flanking DNA-binding domains., The core DNA-binding domain, which comprises both the dimerization domain, and a helix predicted to bind the inner portion of the EBNA1 DNA, recognition element, was remarkably similar to the structure of the, papillomavirus E2 protein, despite a complete lack of sequence, conservation. The flanking DNA-binding domain, only a portion of which is, contained in the current structure, consists in part of an alpha helix, whose N-terminus contacts the outer regions of the EBNA1 DNA recognition, element.

The crystal structure of the DNA-binding and dimerization domains of the Epstein-Barr virus nuclear antigen 1 (EBNA1), which binds to and activates DNA replication from the latent origin of replication in Epstein-Barr virus, was solved at 2.5 A resolution. EBNA1 appears to bind DNA via two independent regions termed the core and the flanking DNA-binding domains. The core DNA-binding domain, which comprises both the dimerization domain and a helix predicted to bind the inner portion of the EBNA1 DNA recognition element, was remarkably similar to the structure of the papillomavirus E2 protein, despite a complete lack of sequence conservation. The flanking DNA-binding domain, only a portion of which is contained in the current structure, consists in part of an alpha helix whose N-terminus contacts the outer regions of the EBNA1 DNA recognition element.

==About this Structure==

1VHI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1VHI OCA].

1VHI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VHI OCA].

==Reference==

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[[Category: origin-binding protein]]

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@@ Line 1: / Line 1: @@
-[[Image:1vhi.gif|left|200px]]<br /><applet load="1vhi" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1vhi.gif|left|200px]]<br /><applet load="1vhi" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1vhi, resolution 2.5&Aring;" />
 '''EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607'''<br />
 ==Overview==
-The crystal structure of the DNA-binding and dimerization domains of the, Epstein-Barr virus nuclear antigen 1 (EBNA1), which binds to and activates, DNA replication from the latent origin of replication in Epstein-Barr, virus, was solved at 2.5 A resolution. EBNA1 appears to bind DNA via two, independent regions termed the core and the flanking DNA-binding domains., The core DNA-binding domain, which comprises both the dimerization domain, and a helix predicted to bind the inner portion of the EBNA1 DNA, recognition element, was remarkably similar to the structure of the, papillomavirus E2 protein, despite a complete lack of sequence, conservation. The flanking DNA-binding domain, only a portion of which is, contained in the current structure, consists in part of an alpha helix, whose N-terminus contacts the outer regions of the EBNA1 DNA recognition, element.
+The crystal structure of the DNA-binding and dimerization domains of the Epstein-Barr virus nuclear antigen 1 (EBNA1), which binds to and activates DNA replication from the latent origin of replication in Epstein-Barr virus, was solved at 2.5 A resolution. EBNA1 appears to bind DNA via two independent regions termed the core and the flanking DNA-binding domains. The core DNA-binding domain, which comprises both the dimerization domain and a helix predicted to bind the inner portion of the EBNA1 DNA recognition element, was remarkably similar to the structure of the papillomavirus E2 protein, despite a complete lack of sequence conservation. The flanking DNA-binding domain, only a portion of which is contained in the current structure, consists in part of an alpha helix whose N-terminus contacts the outer regions of the EBNA1 DNA recognition element.
 ==About this Structure==
-VHI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VHI OCA].
+VHI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VHI OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: origin-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:51:19 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:26 2008''