1vhi

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(New page: 200px<br /><applet load="1vhi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vhi, resolution 2.5&Aring;" /> '''EPSTEIN BARR VIRUS NU...)
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[[Image:1vhi.gif|left|200px]]<br /><applet load="1vhi" size="450" color="white" frame="true" align="right" spinBox="true"
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[[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;" />
caption="1vhi, resolution 2.5&Aring;" />
'''EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607'''<br />
'''EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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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].
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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==
==Reference==
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[[Category: origin-binding protein]]
[[Category: origin-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:51:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:26 2008''

Revision as of 13:35, 21 February 2008


1vhi, resolution 2.5Å

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EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607

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.

About this Structure

1VHI is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.

Reference

Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1., Bochkarev A, Barwell JA, Pfuetzner RA, Furey W Jr, Edwards AM, Frappier L, Cell. 1995 Oct 6;83(1):39-46. PMID:7553871

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