2p1b: Difference between revisions

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New page: left|200px<br /> <applet load="2p1b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p1b, resolution 2.75Å" /> '''Crystal structure o...
 
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[[Image:2p1b.gif|left|200px]]<br />
<applet load="2p1b" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2p1b, resolution 2.75&Aring;" />
'''Crystal structure of human nucleophosmin-core'''<br />


==Disease==
==Crystal structure of human nucleophosmin-core==
Known diseases associated with this structure: Leukemia, acute myeloid OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164040 164040]], Leukemia, acute promyelocytic, NPM/RARA type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164040 164040]]
<StructureSection load='2p1b' size='340' side='right'caption='[[2p1b]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2p1b]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P1B FirstGlance]. <br>
2P1B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2P1B OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#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=2p1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1b OCA], [https://pdbe.org/2p1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p1b RCSB], [https://www.ebi.ac.uk/pdbsum/2p1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p1b ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface., Lee HH, Kim HS, Kang JY, Lee BI, Ha JY, Yoon HJ, Lim SO, Jung G, Suh SW, Proteins. 2007 Nov 15;69(3):672-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17879352 17879352]
== Disease ==
[https://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated.  Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA.  Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1.  Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.
== Function ==
[https://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref>
== 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/p1/2p1b_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/main_output.php?pdb_ID=2p1b ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ha, J.Y.]]
[[Category: Ha JY]]
[[Category: Jung, G.]]
[[Category: Jung G]]
[[Category: Kang, J.Y.]]
[[Category: Kang JY]]
[[Category: Kim, H.S.]]
[[Category: Kim HS]]
[[Category: Lee, B.I.]]
[[Category: Lee BI]]
[[Category: Lee, H.H.]]
[[Category: Lee HH]]
[[Category: Lim, S.O.]]
[[Category: Lim SO]]
[[Category: Suh, S.W.]]
[[Category: Suh SW]]
[[Category: Yoon, H.J.]]
[[Category: Yoon HJ]]
[[Category: chaperone]]
[[Category: decamer]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:19:23 2007''

Latest revision as of 08:58, 25 October 2023

Crystal structure of human nucleophosmin-core

2p1b, resolution 2.75Å

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