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.


2c86

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2c86.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2c86.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2c86| PDB=2c86 | SCENE= }}
{{STRUCTURE_2c86| PDB=2c86 | SCENE= }}
-
'''X-RAY STRUCTURE OF THE N AND C-TERMINAL DOMAIN OF CORONAVIRUS NUCLEOCAPSID PROTEIN.'''
+
===X-RAY STRUCTURE OF THE N AND C-TERMINAL DOMAIN OF CORONAVIRUS NUCLEOCAPSID PROTEIN.===
-
==Overview==
+
<!--
-
Coronaviruses cause a variety of respiratory and enteric diseases in animals and humans including severe acute respiratory syndrome. In these enveloped viruses, the filamentous nucleocapsid is formed by the association of nucleocapsid (N) protein with single-stranded viral RNA. The N protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. We describe the structure of the two proteolytically resistant domains of the N protein from infectious bronchitis virus (IBV), a prototype coronavirus. These domains are located at its N- and C-terminal ends (NTD and CTD, respectively). The NTD of the IBV Gray strain at 1.3-A resolution exhibits a U-shaped structure, with two arms rich in basic residues, providing a module for specific interaction with RNA. The CTD forms a tightly intertwined dimer with an intermolecular four-stranded central beta-sheet platform flanked by alpha helices, indicating that the basic building block for coronavirus nucleocapsid formation is a dimeric assembly of N protein. The variety of quaternary arrangements of the NTD and CTD revealed by the analysis of the different crystal forms delineates possible interfaces that could be used for the formation of a flexible filamentous ribonucleocapsid. The striking similarity between the dimeric structure of CTD and the nucleocapsid-forming domain of a distantly related arterivirus indicates a conserved mechanism of nucleocapsid formation for these two viral families.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16775348}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16775348 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16775348}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Rna-binding]]
[[Category: Rna-binding]]
[[Category: Viral nucleoprotein]]
[[Category: Viral nucleoprotein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:25:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:49:55 2008''

Revision as of 20:49, 28 July 2008

Image:2c86.png

Template:STRUCTURE 2c86

X-RAY STRUCTURE OF THE N AND C-TERMINAL DOMAIN OF CORONAVIRUS NUCLEOCAPSID PROTEIN.

Template:ABSTRACT PUBMED 16775348

About this Structure

2C86 is a Single protein structure of sequence from Infectious bronchitis virus. Full crystallographic information is available from OCA.

Reference

X-ray structures of the N- and C-terminal domains of a coronavirus nucleocapsid protein: implications for nucleocapsid formation., Jayaram H, Fan H, Bowman BR, Ooi A, Jayaram J, Collisson EW, Lescar J, Prasad BV, J Virol. 2006 Jul;80(13):6612-20. PMID:16775348

Page seeded by OCA on Mon Jul 28 23:49:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c86"
Personal tools