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1ifa

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(New page: 200px<br /><applet load="1ifa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifa, resolution 2.6&Aring;" /> '''THREE-DIMENSIONAL CRY...)
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Revision as of 15:14, 20 November 2007

Image:1ifa.jpg

1ifa, resolution 2.6Å

Drag the structure with the mouse to rotate

THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA

Overview

The crystal structure of recombinant murine interferon-beta (IFN-beta) has, been solved by the multiple isomorphous replacement method and refined to, an R-factor of 20.5% against 2.6 A X-ray diffraction data. The structure, shows a variant of the alpha-helix bundle with a new chain-folding, topology, which seems to represent a basic structural framework of all the, IFN-alpha and IFN-beta molecules belonging to the type I family., Functionally important segments of the polypeptide chain, as implied, through numerous gene manipulation studies carried out so far, are, spatially clustered indicating the binding site(s) to the receptor(s)., Comparison of the present structure with those of other alpha-helical, cytokine proteins, including porcine growth hormone, interleukin 2 and, interferon gamma, indicated either a topological similarity in chain, folding or a similar spatial arrangement of the alpha-helices.

About this Structure

1IFA is a Single protein structure of sequence from Mus musculus with ASN as ligand. Full crystallographic information is available from OCA.

Reference

Three-dimensional crystal structure of recombinant murine interferon-beta., Senda T, Shimazu T, Matsuda S, Kawano G, Shimizu H, Nakamura KT, Mitsui Y, EMBO J. 1992 Sep;11(9):3193-201. PMID:1505514

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