2w1o

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{{Seed}}
 
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[[Image:2w1o.png|left|200px]]
 
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==NMR structure of dimerization domain of human ribosomal protein P2==
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The line below this paragraph, containing "STRUCTURE_2w1o", creates the "Structure Box" on the page.
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<StructureSection load='2w1o' size='340' side='right'caption='[[2w1o]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2w1o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W1O FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s4j|1s4j]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w1o OCA], [https://pdbe.org/2w1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w1o RCSB], [https://www.ebi.ac.uk/pdbsum/2w1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w1o ProSAT]</span></td></tr>
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{{STRUCTURE_2w1o| PDB=2w1o | SCENE= }}
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/RLA2_HUMAN RLA2_HUMAN]] Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w1/2w1o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2w1o ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The lateral stalk of ribosome is responsible for kingdom-specific binding of translation factors and activation of GTP hydrolysis that drives protein synthesis. In eukaryotes, the stalk is composed of acidic ribosomal proteins P0, P1 and P2 that constitute a pentameric P-complex in 1: 2: 2 ratio. We have determined the solution structure of the N-terminal dimerization domain of human P2 (NTD-P2), which provides insights into the structural organization of the eukaryotic stalk. Our structure revealed that eukaryotic stalk protein P2 forms a symmetric homodimer in solution, and is structurally distinct from the bacterial counterpart L12 homodimer. The two subunits of NTD-P2 form extensive hydrophobic interactions in the dimeric interface that buries 2400 A(2) of solvent accessible surface area. We have showed that P1 can dissociate P2 homodimer spontaneously to form a more stable P1/P2 1 : 1 heterodimer. By homology modelling, we identified three exposed polar residues on helix-3 of P2 are substituted by conserved hydrophobic residues in P1. Confirmed by mutagenesis, we showed that these residues on helix-3 of P1 are not involved in the dimerization of P1/P2, but instead play a vital role in anchoring P1/P2 heterodimer to P0. Based on our results, models of the eukaryotic stalk complex were proposed.
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===NMR STRUCTURE OF DIMERIZATION DOMAIN OF HUMAN RIBOSOMAL PROTEIN P2===
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Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk.,Lee KM, Yu CW, Chan DS, Chiu TY, Zhu G, Sze KH, Shaw PC, Wong KB Nucleic Acids Res. 2010 Aug;38(15):5206-16. Epub 2010 Apr 12. PMID:20385603<ref>PMID:20385603</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2w1o" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20385603}}, adds the Publication Abstract to the page
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*[[Ribosomal protein P2|Ribosomal protein P2]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20385603 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20385603}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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2W1O is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W1O OCA].
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[[Category: Large Structures]]
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[[Category: Chan, D S]]
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==Reference==
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[[Category: Lee, K M]]
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<ref group="xtra">PMID:20385603</ref><references group="xtra"/>
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[[Category: Shaw, P C]]
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[[Category: Homo sapiens]]
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[[Category: Sze, K H]]
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[[Category: Chan, D S.]]
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[[Category: Wong, K B]]
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[[Category: Lee, K M.]]
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[[Category: Zhu, G]]
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[[Category: Shaw, P C.]]
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[[Category: Sze, K H.]]
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[[Category: Wong, K B.]]
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[[Category: Zhu, G.]]
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[[Category: Dimerization]]
[[Category: Dimerization]]
[[Category: Phosphoprotein]]
[[Category: Phosphoprotein]]
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[[Category: Ribosome]]
[[Category: Ribosome]]
[[Category: Translation]]
[[Category: Translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:55:25 2010''
 

Current revision

NMR structure of dimerization domain of human ribosomal protein P2

PDB ID 2w1o

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