4bbl: Difference between revisions

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OCA

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 ==Cryo-electron microscopy reconstruction of the helical part of influenza A virus ribonucleoprotein isolated from virions.==
-<StructureSection load='4bbl' size='340' side='right' caption='[[4bbl]], [[Resolution|resolution]] 18.00&Aring;' scene=''>
+<SX load='4bbl' size='340' side='right' viewer='molstar' caption='[[4bbl]], [[Resolution|resolution]] 18.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4bbl]] is a 26 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BBL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4bbl]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBL 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=4bbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbl OCA], [http://pdbe.org/4bbl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bbl RCSB], [http://www.ebi.ac.uk/pdbsum/4bbl PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 18&#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=4bbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbl OCA], [https://pdbe.org/4bbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbl RCSB], [https://www.ebi.ac.uk/pdbsum/4bbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbl ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
 == Function ==
-[[http://www.uniprot.org/uniprot/NCAP_I33A0 NCAP_I33A0]] Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus (By similarity).
+[https://www.uniprot.org/uniprot/Q1K9H2_I33A0 Q1K9H2_I33A0] Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus (By similarity).[SAAS:SAAS002141_004_603280]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 20: @@
 ==See Also==
-*[[Nucleoprotein|Nucleoprotein]]
+*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Arranz, R]]
+[[Category: Influenza A virus]]
-[[Category: Carrascosa, J L]]
+[[Category: Large Structures]]
-[[Category: Chichon, F J]]
+[[Category: Arranz R]]
-[[Category: Coloma, R]]
+[[Category: Carrascosa JL]]
-[[Category: Conesa, J J]]
+[[Category: Chichon FJ]]
-[[Category: Martin-Benito, J]]
+[[Category: Coloma R]]
-[[Category: Ortin, J]]
+[[Category: Conesa JJ]]
-[[Category: Valpuesta, J M]]
+[[Category: Martin-Benito J]]
-[[Category: Nuclear protein]]
+[[Category: Ortin J]]
-[[Category: Nucleocapsid]]
+[[Category: Valpuesta JM]]