1nlq

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{{STRUCTURE_1nlq| PDB=1nlq | SCENE= }}
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'''The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding'''
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===The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding===
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==Overview==
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The nucleoplasmin-like protein from Drosophila (dNLP) functions as a chaperone for core histones and may remodel chromatin in embryos. We now report the crystal structure of a dNLP-core pentamer at 1.5 A resolution. The monomer has an eight-stranded, beta barrel topology that is similar to nucleoplasmin (Np). However, a signature beta hairpin is tucked in along the lateral surface of the dNLP-core pentamer, while it extends outward in the Np-core decamer. Drosophila NLP and Np both assemble histone octamers. This process may require each chaperone to form a decamer, which would create symmetric binding sites for the histones. Conformational differences between dNLP and Np may reflect their different oligomeric states, while a conserved, nonpolar subunit interface may allow conformational plasticity during histone binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 12575937 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12575937}}
==About this Structure==
==About this Structure==
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[[Category: Nucleoplasmin]]
[[Category: Nucleoplasmin]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:40:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:12:33 2008''

Revision as of 12:12, 28 July 2008

Image:1nlq.png

Template:STRUCTURE 1nlq

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding

Template:ABSTRACT PUBMED 12575937

About this Structure

1NLQ is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding., Namboodiri VM, Dutta S, Akey IV, Head JF, Akey CW, Structure. 2003 Feb;11(2):175-86. PMID:12575937

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