1nlq
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(New page: 200px<br /><applet load="1nlq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nlq, resolution 1.50Å" /> '''The crystal structur...)
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Revision as of 20:15, 20 November 2007
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The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
Overview
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.
About this Structure
1NLQ is a Single protein structure of sequence from Drosophila melanogaster with MG as ligand. 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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