1ejy: Difference between revisions

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New page: left|200px<br /><applet load="1ejy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejy, resolution 2.90Å" /> '''MOUSE IMPORTIN ALPHA...
 
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[[Image:1ejy.gif|left|200px]]<br /><applet load="1ejy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ejy, resolution 2.90&Aring;" />
'''MOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX'''<br />


==Overview==
==MOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX==
Importin-alpha is the nuclear import receptor that recognizes cargo, proteins which contain classical monopartite and bipartite nuclear, localization sequences (NLSs), and facilitates their transport into the, nucleus. To determine the structural basis of the recognition of the two, classes of NLSs by mammalian importin-alpha, we co-crystallized an, N-terminally truncated mouse receptor protein with peptides corresponding, to the monopartite NLS from the simian virus 40 (SV40) large T-antigen, and the bipartite NLS from nucleoplasmin. We show that the monopartite, SV40 large T-antigen NLS binds to two binding sites on the receptor, similar to what was observed in yeast importin-alpha. The nucleoplasmin, NLS-importin-alpha complex shows, for the first time, the mode of binding, of bipartite NLSs to the receptor. The two basic clusters in the NLS, occupy the two binding sites used by the monopartite NLS, while the, sequence linking the two basic clusters is poorly ordered, consistent with, its tolerance to mutations. The structures explain the structural basis, for binding of diverse NLSs to the sole receptor protein.
<StructureSection load='1ejy' size='340' side='right'caption='[[1ejy]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ejy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EJY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#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=1ejy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ejy OCA], [https://pdbe.org/1ejy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ejy RCSB], [https://www.ebi.ac.uk/pdbsum/1ejy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ejy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NUPL_XENLA NUPL_XENLA] Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Nucleoplasmin is an acidic protein which is able to assemble nucleosomes by binding histones and transferring them to DNA.
== 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/ej/1ejy_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=1ejy ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJY OCA].
*[[Importin 3D structures|Importin 3D structures]]
 
*[[Nucleoplasmin|Nucleoplasmin]]
==Reference==
__TOC__
Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha., Fontes MR, Teh T, Kobe B, J Mol Biol. 2000 Apr 14;297(5):1183-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10764582 10764582]
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Xenopus laevis]]
[[Category: Fontes, M.R.]]
[[Category: Fontes MR]]
[[Category: Kobe, B.]]
[[Category: Kobe B]]
[[Category: Teh, T.]]
[[Category: Teh T]]
[[Category: importin aplpha/karyopherin alpha; nuclear localization sequence (nls) recognition; nucleoplasmin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:04:10 2007''

Latest revision as of 10:03, 7 February 2024

MOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEXMOUSE IMPORTIN ALPHA-NUCLEOPLASMIN NLS PEPTIDE COMPLEX

Structural highlights

1ejy is a 2 chain structure with sequence from Mus musculus and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NUPL_XENLA Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Nucleoplasmin is an acidic protein which is able to assemble nucleosomes by binding histones and transferring them to DNA.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1ejy, resolution 2.90Å

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