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[[Image: | ==P1 Crystal structure of the N-terminal R1-R7 of murine MVP== | ||
<StructureSection load='3gnf' size='340' side='right' caption='[[3gnf]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3gnf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GNF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GNF FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gf5|3gf5]], [[3gng|3gng]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mvp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3gnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gnf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gnf RCSB], [http://www.ebi.ac.uk/pdbsum/3gnf PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gn/3gnf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel-shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data indicated that vault halves can dissociate at acidic pH. The crystal structure of the vault particle solved at 8 A resolution, together with the 2.1-A structure of the seven N-terminal domains (R1-R7) of MVP, reveal the interactions governing vault association and provide an explanation for a reversible dissociation induced by low pH. The structural comparison with the recently published 3.5 A model shows major discrepancies, both in the main chain tracing and in the side chain assignment of the two terminal domains R1 and R2. | |||
The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP.,Querol-Audi J, Casanas A, Uson I, Luque D, Caston JR, Fita I, Verdaguer N EMBO J. 2009 Nov 4;28(21):3450-7. Epub 2009 Sep 24. PMID:19779459<ref>PMID:19779459</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Casanas, A | [[Category: Casanas, A]] | ||
[[Category: Caston, J R | [[Category: Caston, J R]] | ||
[[Category: Fita, I | [[Category: Fita, I]] | ||
[[Category: Luque, D | [[Category: Luque, D]] | ||
[[Category: Querol-Audi, J | [[Category: Querol-Audi, J]] | ||
[[Category: Uson, I | [[Category: Uson, I]] | ||
[[Category: Verdaguer, N | [[Category: Verdaguer, N]] | ||
[[Category: Beta sheet]] | [[Category: Beta sheet]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Ribonucleoprotein]] | [[Category: Ribonucleoprotein]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
Revision as of 12:37, 8 December 2014
P1 Crystal structure of the N-terminal R1-R7 of murine MVPP1 Crystal structure of the N-terminal R1-R7 of murine MVP
Structural highlights
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 PubMedVaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel-shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data indicated that vault halves can dissociate at acidic pH. The crystal structure of the vault particle solved at 8 A resolution, together with the 2.1-A structure of the seven N-terminal domains (R1-R7) of MVP, reveal the interactions governing vault association and provide an explanation for a reversible dissociation induced by low pH. The structural comparison with the recently published 3.5 A model shows major discrepancies, both in the main chain tracing and in the side chain assignment of the two terminal domains R1 and R2. The mechanism of vault opening from the high resolution structure of the N-terminal repeats of MVP.,Querol-Audi J, Casanas A, Uson I, Luque D, Caston JR, Fita I, Verdaguer N EMBO J. 2009 Nov 4;28(21):3450-7. Epub 2009 Sep 24. PMID:19779459[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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