1a92

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1a92" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a92, resolution 1.8&Aring;" /> '''OLIGOMERIZATION DOMAI...)
Current revision (06:28, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1a92.gif|left|200px]]<br /><applet load="1a92" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1a92, resolution 1.8&Aring;" />
 
-
'''OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN'''<br />
 
-
==Overview==
+
==OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN==
-
BACKGROUND: The hepatitis D virus (HDV) is a small satellite virus of, hepatitis B virus (HBV). Coinfection with HBV and HDV causes severe liver, disease in humans. The small 195 amino-acid form of the hepatitis delta, antigen (HDAg) functions as a trans activator of HDV replication. A larger, form of the protein containing a 19 amino acid C-terminal extension, inhibits viral replication. Both of these functions are mediated in part, by a stretch of amino acids predicted to form a coiled coil (residues, 13-48) that is common to both forms. It is believed that HDAg forms dimers, and higher ordered structures through this coiled-coil region. RESULTS:, The high-resolution crystal structure of a synthetic peptide corresponding, to residues 12 to 60 of HDAg has been solved. The peptide forms an, antiparallel coiled coil, with hydrophobic residues near the termini of, each peptide forming an extensive hydrophobic core with residues, C-terminal to the coiled-coil domain in the dimer protein. The structure, shows how HDAg forms dimers, but also shows the dimers forming an octamer, that forms a 50 A ring lined with basic sidechains. This is confirmed by, cross-linking studies of full-length recombinant small HDAg. CONCLUSIONS:, HDAg dimerizes through an antiparallel coiled coil. Dimers then associate, further to form octamers through residues in the coiled-coil domain and, residues C-terminal to this region. Our findings suggest that the, structure of HDAg represents a previously unseen organization of a, nucleocapsid protein and raise the possibility that the N terminus may, play a role in binding the viral RNA.
+
<StructureSection load='1a92' size='340' side='right'caption='[[1a92]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1a92]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_delta_virus Hepatitis delta virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A92 FirstGlance]. <br>
-
1A92 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_delta_virus Hepatitis delta virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A92 OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
 
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a92 OCA], [https://pdbe.org/1a92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a92 RCSB], [https://www.ebi.ac.uk/pdbsum/1a92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a92 ProSAT]</span></td></tr>
-
==Reference==
+
</table>
-
Structural basis of the oligomerization of hepatitis delta antigen., Zuccola HJ, Rozzelle JE, Lemon SM, Erickson BW, Hogle JM, Structure. 1998 Jul 15;6(7):821-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9687364 9687364]
+
== Function ==
 +
[https://www.uniprot.org/uniprot/SHDAG_HDVAM SHDAG_HDVAM] Promotes both transcription and replication of genomic RNA. Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. May interact with host RNA polymerase II thereby changing its template requirement from DNA to RNA. RNA pol II complex would then acts as an RNA-directed RNA polymerase, and transcribe and replicate HDV genome (By similarity).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a9/1a92_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a92 ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Hepatitis delta virus]]
[[Category: Hepatitis delta virus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Hogle, J.M.]]
+
[[Category: Hogle JM]]
-
[[Category: Zuccola, H.J.]]
+
[[Category: Zuccola HJ]]
-
[[Category: coiled-coil]]
+
-
[[Category: hdv]]
+
-
[[Category: hepatitis delta]]
+
-
[[Category: leucine zipper]]
+
-
[[Category: oligomerization]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:41:32 2007''
+

Current revision

OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN

PDB ID 1a92

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a92"
Personal tools