1wu3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1wu3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wu3, resolution 2.15&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:1wu3.jpg|left|200px]]<br /><applet load="1wu3" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1wu3.jpg|left|200px]]<br /><applet load="1wu3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wu3, resolution 2.15&Aring;" />
caption="1wu3, resolution 2.15&Aring;" />
'''Crystal structure of recombinant murine interferon beta'''<br />
'''Crystal structure of recombinant murine interferon beta'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1WU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure superseeds the now removed PDB entry 1RMI. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WU3 OCA].
+
1WU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry 1RMI. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WU3 OCA].
==Reference==
==Reference==
Line 18: Line 18:
[[Category: alpha-helix-bundle]]
[[Category: alpha-helix-bundle]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:40:32 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:09 2008''

Revision as of 13:48, 21 February 2008


1wu3, resolution 2.15Å

Drag the structure with the mouse to rotate

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 supersedes 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

Page seeded by OCA on Thu Feb 21 15:48:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools