1knz

From Proteopedia

(Difference between revisions)

Revision as of 21:21, 24 January 2018

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer

Structural highlights

1knz is a 12 chain structure with sequence from Simian 11 rotavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NSP3_ROTS1] Involved in the shutoff of host protein synthesis. It is unclear whether it is required for the translation of viral mRNAs as well. Functions similarly to, and competes with the cellular poly(A)-binding protein PABPC1. Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs and allows circularization of viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with the eukaryotic translation initiation factor eIF4G, using the same region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the translation of cellular poly(A) mRNAs. Also responsible for the nuclear relocalization of PABPC1 upon rotavirus infection (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Rotaviruses, the cause of life-threatening diarrhea in humans and cattle, utilize a functional homolog of poly(A) binding protein (PABP) known as nonstructural protein 3 (NSP3) for translation of viral mRNAs. NSP3 binds to viral mRNA 3' consensus sequences and circularizes the mRNA via interactions with eIF4G. The X-ray structure of the NSP3 RNA binding domain bound to a rotaviral mRNA 3' end has been determined. NSP3 is a novel, heart-shaped homodimer with a medial RNA binding cleft. The homodimer is asymmetric, and contains two similar N-terminal segments plus two structurally different C-terminal segments that intertwine to create a tunnel enveloping the mRNA 3' end. Biophysical studies demonstrate high affinity binding leading to increased thermal stability and slow dissociation kinetics, consistent with NSP3 function.

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer.,Deo RC, Groft CM, Rajashankar KR, Burley SK Cell. 2002 Jan 11;108(1):71-81. PMID:11792322^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Deo RC, Groft CM, Rajashankar KR, Burley SK. Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Cell. 2002 Jan 11;108(1):71-81. PMID:11792322

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1knz"

@@ Line 1: / Line 1: @@
 ==Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer==
 <StructureSection load='1knz' size='340' side='right' caption='[[1knz]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1knz]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Simian_11_rotavirus Simian 11 rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KNZ FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1knz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knz OCA], [http://pdbe.org/1knz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1knz RCSB], [http://www.ebi.ac.uk/pdbsum/1knz PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1knz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knz OCA], [http://pdbe.org/1knz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1knz RCSB], [http://www.ebi.ac.uk/pdbsum/1knz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1knz ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1knz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1knz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 26: / Line 27: @@
 </div>
 <div class="pdbe-citations 1knz" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Nonstructural protein|Nonstructural protein]]
 == References ==
 <references/>

1knz

From Proteopedia

Revision as of 21:21, 24 January 2018

Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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