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.


2gtt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:13, 18 October 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='2gtt' size='340' side='right'caption='[[2gtt]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
<StructureSection load='2gtt' size='340' side='right'caption='[[2gtt]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2gtt]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Rabies_virus Rabies virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GTT FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2gtt]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Rabies_lyssavirus Rabies lyssavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GTT FirstGlance]. <br>
-
</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=2gtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gtt OCA], [https://pdbe.org/2gtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gtt RCSB], [https://www.ebi.ac.uk/pdbsum/2gtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gtt ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.49&#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=2gtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gtt OCA], [https://pdbe.org/2gtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gtt RCSB], [https://www.ebi.ac.uk/pdbsum/2gtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gtt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/NCAP_RABVE NCAP_RABVE]] Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).
+
[https://www.uniprot.org/uniprot/NCAP_RABVE NCAP_RABVE] Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 25: Line 26:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Rabies virus]]
+
[[Category: Rabies lyssavirus]]
-
[[Category: Albertini, A A.V]]
+
[[Category: Albertini AAV]]
-
[[Category: Muziol, T]]
+
[[Category: Muziol T]]
-
[[Category: Ravelli, R B.G]]
+
[[Category: Ravelli RBG]]
-
[[Category: Ruigrok, R W.H]]
+
[[Category: Ruigrok RWH]]
-
[[Category: Weissenhorn, W]]
+
[[Category: Weissenhorn W]]
-
[[Category: Wernimont, A K]]
+
[[Category: Wernimont AK]]
-
[[Category: Nucleoprotein]]
+
-
[[Category: Protein-rna complex]]
+
-
[[Category: Rna binding protein]]
+
-
[[Category: Viral protein]]
+

Current revision

Crystal structure of the rabies virus nucleoprotein-RNA complex

PDB ID 2gtt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools