2c9n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2c9n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c9n, resolution 3.3&Aring;" /> '''STRUCTURE OF THE EPST...)
Line 1: Line 1:
-
[[Image:2c9n.gif|left|200px]]<br /><applet load="2c9n" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2c9n.gif|left|200px]]<br /><applet load="2c9n" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2c9n, resolution 3.3&Aring;" />
caption="2c9n, resolution 3.3&Aring;" />
'''STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN AT APPROXIMATELY 3.5 ANGSTROM RESOLUTION'''<br />
'''STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN AT APPROXIMATELY 3.5 ANGSTROM RESOLUTION'''<br />
==Overview==
==Overview==
-
Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to, several human malignancies. EBV has a biphasic infection cycle consisting, of a latent and a lytic, replicative phase. The switch from latent to, lytic infection is triggered by the EBV immediate-early transcription, factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of, ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element., ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in, which a C-terminal moiety stabilizes the coiled coil involved in dimer, formation. The structure provides insights into ZEBRA's broad target site, specificity, preferential activation of specific EBV promoters in their, methylated state, ability to dimerize despite lacking a leucine zipper, motif, and failure to heterodimerize with cellular bZIP proteins. The, structure will allow for the design of new therapeutic agents that block, activation of the EBV lytic cycle.
+
Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to several human malignancies. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element. ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in which a C-terminal moiety stabilizes the coiled coil involved in dimer formation. The structure provides insights into ZEBRA's broad target site specificity, preferential activation of specific EBV promoters in their methylated state, ability to dimerize despite lacking a leucine zipper motif, and failure to heterodimerize with cellular bZIP proteins. The structure will allow for the design of new therapeutic agents that block activation of the EBV lytic cycle.
==About this Structure==
==About this Structure==
-
2C9N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2C9N OCA].
+
2C9N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2C9N OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Human herpesvirus 4]]
[[Category: Human herpesvirus 4]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Artero, J.B.]]
+
[[Category: Artero, J B.]]
[[Category: Baudin, F.]]
[[Category: Baudin, F.]]
[[Category: Morand, P.]]
[[Category: Morand, P.]]
[[Category: Moulin, M.]]
[[Category: Moulin, M.]]
-
[[Category: Muller, C.W.]]
+
[[Category: Muller, C W.]]
[[Category: Petosa, C.]]
[[Category: Petosa, C.]]
[[Category: bzip protein]]
[[Category: bzip protein]]
Line 31: Line 31:
[[Category: zta]]
[[Category: zta]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:03:23 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:29 2008''

Revision as of 14:46, 21 February 2008


2c9n, resolution 3.3Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN AT APPROXIMATELY 3.5 ANGSTROM RESOLUTION

Overview

Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to several human malignancies. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element. ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in which a C-terminal moiety stabilizes the coiled coil involved in dimer formation. The structure provides insights into ZEBRA's broad target site specificity, preferential activation of specific EBV promoters in their methylated state, ability to dimerize despite lacking a leucine zipper motif, and failure to heterodimerize with cellular bZIP proteins. The structure will allow for the design of new therapeutic agents that block activation of the EBV lytic cycle.

About this Structure

2C9N is a Protein complex structure of sequences from Human herpesvirus 4. Full crystallographic information is available from OCA.

Reference

Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein., Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW, Mol Cell. 2006 Feb 17;21(4):565-72. PMID:16483937

Page seeded by OCA on Thu Feb 21 16:46:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools