1oks

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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:48:50 2007''
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Revision as of 13:52, 30 October 2007


1oks, resolution 1.80Å

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CRYSTAL STRUCTURE OF THE MEASLES VIRUS PHOSPHOPROTEIN XD DOMAIN

Overview

Measles virus is a negative-sense, single-stranded RNA virus belonging to, the Mononegavirales order which comprises several human pathogens such as, Ebola, Nipah, and Hendra viruses. The phosphoprotein of measles virus is a, modular protein consisting of an intrinsically disordered N-terminal, domain (Karlin, D., Longhi, S., Receveur, V., and Canard, B. (2002), Virology 296, 251-262) and of a C-terminal moiety (PCT) composed of, alternating disordered and globular regions. We report the crystal, structure of the extreme C-terminal domain (XD) of measles virus, phosphoprotein (aa 459-507) at 1.8 A resolution. We have previously, reported that the C-terminal domain of measles virus nucleoprotein, NTAIL, is intrinsically unstructured and undergoes induced folding in the, presence of PCT ... [(full description)]

About this Structure

1OKS is a [Single protein] structure of sequence from [Measles virus] with NHE as [ligand]. Active as [RNA-directed RNA polymerase], with EC number [2.7.7.48]. Structure known Active Site: NHE. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein., Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S, J Biol Chem. 2003 Nov 7;278(45):44567-73. Epub 2003 Aug 27. PMID:12944395

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