This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a92

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a92.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a92.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a92| PDB=1a92 | SCENE= }}
{{STRUCTURE_1a92| PDB=1a92 | SCENE= }}
-
'''OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN'''
+
===OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9687364}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9687364 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9687364}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Leucine zipper]]
[[Category: Leucine zipper]]
[[Category: Oligomerization]]
[[Category: Oligomerization]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:59:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:24:33 2008''

Revision as of 13:24, 30 June 2008

Image:1a92.png

Template:STRUCTURE 1a92

OLIGOMERIZATION DOMAIN OF HEPATITIS DELTA ANTIGEN

Template:ABSTRACT PUBMED 9687364

About this Structure

1A92 is a Single protein structure of sequence from Hepatitis delta virus. Full crystallographic information is available from OCA.

Reference

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:9687364

Page seeded by OCA on Mon Jun 30 16:24:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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