2bt7
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(New page: 200px<br /> <applet load="2bt7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bt7, resolution 2.35Å" /> '''STRUCTURE OF THE C-...)
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Revision as of 19:52, 29 October 2007
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STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN REOVIRUS FIBRE SIGMAC, CD CRYSTAL FORM
Overview
Avian reovirus fibre, a homo-trimer of the sigmaC protein, is responsible, for primary host cell attachment. The protein expressed in bacteria forms, elongated fibres comprised of a carboxy-terminal globular head domain and, a slender shaft, and partial proteolysis yielded a carboxy-terminal, protease-stable domain that was amenable to crystallisation. Here, we show, that this fragment retains receptor-binding capability and report its, structure, solved using two-wavelength anomalous diffraction and refined, using data collected from three different crystal forms at 2.1 angstroms, 2.35 angstroms and 3.0 angstroms resolution. The carboxy-terminal globular, domain has a beta-barrel fold with the same overall topology as the, mammalian reovirus fibre (sigma1). However, the monomers of the ... [(full description)]
About this Structure
2BT7 is a [Single protein] structure of sequence from [Avian orthoreovirus] with SO4 and CD as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structure of the carboxy-terminal receptor-binding domain of avian reovirus fibre sigmaC., Guardado Calvo P, Fox GC, Hermo Parrado XL, Llamas-Saiz AL, Costas C, Martinez-Costas J, Benavente J, van Raaij MJ, J Mol Biol. 2005 Nov 18;354(1):137-49. Epub 2005 Sep 30. PMID:16236316
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