1wu3

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1wu3, resolution 2.15Å

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Crystal structure of recombinant murine interferon beta

Overview

The crystal structure of recombinant murine interferon-beta (reMuIFN-beta), has been refined at 2.15 A resolution using newly collected synchrotron, data. Based on 11,228 reflections (8.0 to 2.15 A), a final R-factor of, 19.1% (with a free R-factor of 25.8%) was obtained with a model obeying, standard geometry within 0.013 A in bond lengths and 1.4 degrees in bond, angles. Compared with the previously reported model, several amino acid, residues in helix A are frame-shifted, the conformations are changed for, parts of loops AB and BC, helix C is extended and a new short helix exists, in loop CD. Evolutionary considerations taken together, the type I, interferons appear to share common structural features with respect to the, chain-folding topology and the hydrogen-bond networks between various, polypeptide segments. Specifically, the disposition of the C-terminal, segment of loop AB (after Arg33), known to be an important, receptor-binding site, seems to be strictly maintained among the type I, interferons. The exposed amino acid residues on helices A and C, which, have recently been implicated as the binding site for another receptor, molecule, are less well conserved. This may be responsible for varied, cellular effects among the subtypes of type I interferons.

About this Structure

1WU3 is a Single protein structure of sequence from Mus musculus. This structure superseeds the now removed PDB entry 1RMI. Full crystallographic information is available from OCA.

Reference

Refined crystal structure of recombinant murine interferon-beta at 2.15 A resolution., Senda T, Saitoh S, Mitsui Y, J Mol Biol. 1995 Oct 13;253(1):187-207. PMID:7473712

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