4v60: Difference between revisions

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<StructureSection load='4v60' size='340' side='right'caption='[[4v60]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='4v60' size='340' side='right'caption='[[4v60]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4v60]] is a 39 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zuo 2zuo], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zv4 2zv4] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zv5 2zv5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V60 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4v60]] is a 39 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zuo 2zuo], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zv4 2zv4] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zv5 2zv5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V60 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=4v60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v60 OCA], [http://pdbe.org/4v60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v60 RCSB], [http://www.ebi.ac.uk/pdbsum/4v60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v60 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]] 3.5&#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=4v60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v60 OCA], [https://pdbe.org/4v60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v60 RCSB], [https://www.ebi.ac.uk/pdbsum/4v60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v60 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MVP_RAT MVP_RAT]] Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity).  
[https://www.uniprot.org/uniprot/MVP_RAT MVP_RAT] Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vaults are among the largest cytoplasmic ribonucleoprotein particles and are found in numerous eukaryotic species. Roles in multidrug resistance and innate immunity have been suggested, but the cellular function remains unclear. We have determined the x-ray structure of rat liver vault at 3.5 angstrom resolution and show that the cage structure consists of a dimer of half-vaults, with each half-vault comprising 39 identical major vault protein (MVP) chains. Each MVP monomer folds into 12 domains: nine structural repeat domains, a shoulder domain, a cap-helix domain, and a cap-ring domain. Interactions between the 42-turn-long cap-helix domains are key to stabilizing the particle. The shoulder domain is structurally similar to a core domain of stomatin, a lipid-raft component in erythrocytes and epithelial cells.
 
The structure of rat liver vault at 3.5 angstrom resolution.,Tanaka H, Kato K, Yamashita E, Sumizawa T, Zhou Y, Yao M, Iwasaki K, Yoshimura M, Tsukihara T Science. 2009 Jan 16;323(5912):384-8. PMID:19150846<ref>PMID:19150846</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4v60" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Major vault protein|Major vault protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Kato, K]]
[[Category: Kato K]]
[[Category: Tanaka, H]]
[[Category: Tanaka H]]
[[Category: Tsukihara, T]]
[[Category: Tsukihara T]]
[[Category: Yamashita, E]]
[[Category: Yamashita E]]
[[Category: Yao, M]]
[[Category: Yao M]]
[[Category: Yoshimura, M]]
[[Category: Yoshimura M]]
[[Category: Zhou, Y]]
[[Category: Zhou Y]]
[[Category: Repeat domain]]
[[Category: Protein-protein complex]]
[[Category: Ribonucleoprotein]]
[[Category: Structural protein]]

Latest revision as of 09:01, 20 March 2024

The structure of rat liver vault at 3.5 angstrom resolution

4v60, resolution 3.50Å

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