1ifa: Difference between revisions

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New page: left|200px<br /><applet load="1ifa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifa, resolution 2.6Å" /> '''THREE-DIMENSIONAL CRY...
 
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[[Image:1ifa.jpg|left|200px]]<br /><applet load="1ifa" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ifa.jpg|left|200px]]<br /><applet load="1ifa" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ifa, resolution 2.6&Aring;" />
caption="1ifa, resolution 2.6&Aring;" />
'''THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA'''<br />
'''THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA'''<br />


==Overview==
==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.
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==
==About this Structure==
1IFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ASN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IFA OCA].  
1IFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ASN:'>ASN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFA OCA].  


==Reference==
==Reference==
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[[Category: Matsuda, S.]]
[[Category: Matsuda, S.]]
[[Category: Mitsui, Y.]]
[[Category: Mitsui, Y.]]
[[Category: Nakamura, K.T.]]
[[Category: Nakamura, K T.]]
[[Category: Senda, T.]]
[[Category: Senda, T.]]
[[Category: Shimizu, H.]]
[[Category: Shimizu, H.]]
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[[Category: glycoprotein]]
[[Category: glycoprotein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:21:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:20 2008''

Revision as of 14:11, 21 February 2008

File:1ifa.jpg


1ifa, resolution 2.6Å

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THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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