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1k5j

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[[Image:1k5j.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1k5j", creates the "Structure Box" on the page.
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|GENE= Nucleoplasmin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k5j OCA], [http://www.ebi.ac.uk/pdbsum/1k5j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k5j RCSB]</span>
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'''The Crystal Structure of Nucleoplasmin-Core'''
'''The Crystal Structure of Nucleoplasmin-Core'''
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[[Category: Laue, T.]]
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[[Category: Nolte, R T.]]
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[[Category: beta-barrel]]
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[[Category: Beta-barrel]]
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[[Category: beta-bulge]]
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[[Category: Beta-bulge]]
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[[Category: jellyroll]]
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Revision as of 19:20, 2 May 2008

Template:STRUCTURE 1k5j

The Crystal Structure of Nucleoplasmin-Core


Overview

The efficient assembly of histone complexes and nucleosomes requires the participation of molecular chaperones. Currently, there is a paucity of data on their mechanism of action. We now present the structure of an N-terminal domain of nucleoplasmin (Np-core) at 2.3 A resolution. The Np-core monomer is an eight-stranded beta barrel that fits snugly within a stable pentamer. In the crystal, two pentamers associate to form a decamer. We show that both Np and Np-core are competent to assemble large complexes that contain the four core histones. Further experiments and modeling suggest that these complexes each contain five histone octamers which dock to a central Np decamer. This work has important ramifications for models of histone storage, sperm chromatin decondensation, and nucleosome assembly.

About this Structure

1K5J is a Single protein structure of sequence from Xenopus laevis. The following page contains interesting information on the relation of 1K5J with [Importins]. Full crystallographic information is available from OCA.

Reference

The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly., Dutta S, Akey IV, Dingwall C, Hartman KL, Laue T, Nolte RT, Head JF, Akey CW, Mol Cell. 2001 Oct;8(4):841-53. PMID:11684019 Page seeded by OCA on Fri May 2 22:20:12 2008

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