3t30: Difference between revisions
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[[ | ==Human nucleoplasmin (Npm2): a histone chaperone in oocytes and early embryos== | ||
<StructureSection load='3t30' size='340' side='right' caption='[[3t30]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t30]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T30 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NPM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3t30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t30 RCSB], [http://www.ebi.ac.uk/pdbsum/3t30 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human Npm2 is an ortholog of Xenopus nucleoplasmin (Np), a chaperone that binds histones. We have determined the crystal structure of a truncated Npm2-core at 1.9 A resolution and show that the N-terminal domains of Npm2 and Np form similar pentamers. This allowed us to model an Npm2 decamer which may be formed by hydrogen bonds between quasi-conserved residues in the interface between two pentamers. Interestingly, the Npm2 pentamer lacks a prototypical A1-acidic tract in each of its subunits. This feature may be responsible for the inability of Npm2-core to bind histones. However, Npm2 with a large acidic tract in its C-terminal tail (Npm2-A2) is able to bind histones and form large complexes. Fluorescence resonance energy transfer experiments and biochemical analysis of loop mutations support the premise that nucleoplasmins form decamers when they bind H2A-H2B dimers and H3-H4 tetramers simultaneously. In the absence of histone tetramers, these chaperones bind H2A-H2B dimers with a single pentamer forming the central hub. When taken together, our data provide insights into the mechanism of histone binding by nucleoplasmins. | |||
Crystal Structure and Function of Human Nucleoplasmin (Npm2): A Histone Chaperone in Oocytes and Embryos.,Platonova O, Akey IV, Head JF, Akey CW Biochemistry. 2011 Sep 20;50(37):8078-8089. Epub 2011 Aug 24. PMID:21863821<ref>PMID:21863821</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Nucleoplasmin|Nucleoplasmin]] | *[[Nucleoplasmin|Nucleoplasmin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Akey, C W | [[Category: Akey, C W]] | ||
[[Category: Head, J F | [[Category: Head, J F]] | ||
[[Category: Platonova, O | [[Category: Platonova, O]] | ||
[[Category: Beta-barrel jelly roll topology]] | [[Category: Beta-barrel jelly roll topology]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
Revision as of 12:45, 9 December 2014
Human nucleoplasmin (Npm2): a histone chaperone in oocytes and early embryos
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