2ayu

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[[Image:2ayu.gif|left|200px]]
[[Image:2ayu.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2ayu", creates the "Structure Box" on the page.
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|GENE= NAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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{{STRUCTURE_2ayu| PDB=2ayu | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ayu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayu OCA], [http://www.ebi.ac.uk/pdbsum/2ayu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ayu RCSB]</span>
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'''The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling'''
'''The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling'''
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[[Category: Luger, K.]]
[[Category: Luger, K.]]
[[Category: Park, Y J.]]
[[Category: Park, Y J.]]
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[[Category: histone chaperone]]
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[[Category: Histone chaperone]]
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[[Category: nucleosome assembly protein 1 (nap1)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:38:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:59:09 2008''
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Revision as of 16:38, 3 May 2008

Template:STRUCTURE 2ayu

The structure of nucleosome assembly protein suggests a mechanism for histone binding and shuttling


Overview

Nucleosome assembly protein 1 (NAP-1) is an integral component in the establishment, maintenance, and dynamics of eukaryotic chromatin. It shuttles histones into the nucleus, assembles nucleosomes, and promotes chromatin fluidity, thereby affecting the transcription of many genes. The 3.0 A crystal structure of yeast NAP-1 reveals a previously uncharacterized fold with implications for histone binding and shuttling. A long alpha-helix is responsible for homodimerization via a previously uncharacterized antiparallel non-coiled-coil, and an alpha/beta domain is implicated in protein-protein interaction. A nuclear export sequence that is embedded in the dimerization helix is almost completely masked by an accessory domain that contains several target sites for casein kinase II. The four-stranded antiparallel beta-sheet that characterizes the alpha/beta domain is found in all histone chaperones, despite the absence of homology in sequence, structural context, or quaternary structure. To our knowledge, this is the first structure of a member of the large NAP family of proteins and suggests a mechanism by which the shuttling of histones to and from the nucleus is regulated.

About this Structure

2AYU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The structure of nucleosome assembly protein 1., Park YJ, Luger K, Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1248-53. Epub 2006 Jan 23. PMID:16432217 Page seeded by OCA on Sat May 3 19:38:24 2008

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