1rfb

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(New page: 200px<br /><applet load="1rfb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rfb, resolution 3.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1rfb.gif|left|200px]]<br /><applet load="1rfb" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1rfb, resolution 3.0&Aring;" />
'''CRYSTAL STRUCTURE OF RECOMBINANT BOVINE INTERFERON-GAMMA AT 3.0 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF RECOMBINANT BOVINE INTERFERON-GAMMA AT 3.0 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The three-dimensional crystal structure of recombinant bovine, interferon-gamma was determined using the multiple isomorphous replacement, method at 3.0 A and refined to an R factor of 19.2%. This protein, crystallizes in space group P2(1)2(1)2(1) with unit-cell parameters of a =, 42.8, b = 79.9 and c = 85.4 A. There is one functional dimer in the, asymmetric unit. The two polypeptide chains are related by a, non-crystallographic twofold symmetry axis. The secondary structure is, predominantly alpha-helical with extensive interdigitation of the, alpha-helical segments of the polypeptide chains that make up the dimer., The secondary structure, tertiary structure and topology of this molecule, are identical to the previously reported structures of recombinant rabbit, interferon-gamma and recombinant human interferon-gamma. The molecular, topology is also similar to that of murine interferon-beta. These, structural similarities strongly indicate the presence of a unique, topological feature (fold) among gamma-interferons from different species, and also among the different classes of interferons.
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The three-dimensional crystal structure of recombinant bovine interferon-gamma was determined using the multiple isomorphous replacement method at 3.0 A and refined to an R factor of 19.2%. This protein crystallizes in space group P2(1)2(1)2(1) with unit-cell parameters of a = 42.8, b = 79.9 and c = 85.4 A. There is one functional dimer in the asymmetric unit. The two polypeptide chains are related by a non-crystallographic twofold symmetry axis. The secondary structure is predominantly alpha-helical with extensive interdigitation of the alpha-helical segments of the polypeptide chains that make up the dimer. The secondary structure, tertiary structure and topology of this molecule are identical to the previously reported structures of recombinant rabbit interferon-gamma and recombinant human interferon-gamma. The molecular topology is also similar to that of murine interferon-beta. These structural similarities strongly indicate the presence of a unique topological feature (fold) among gamma-interferons from different species, and also among the different classes of interferons.
==About this Structure==
==About this Structure==
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1RFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RFB OCA].
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1RFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFB OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rubin, J.R.]]
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[[Category: Rubin, J R.]]
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[[Category: Samudzi, C.T.]]
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[[Category: Samudzi, C T.]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:33:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:15 2008''

Revision as of 12:50, 21 February 2008


1rfb, resolution 3.0Å

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CRYSTAL STRUCTURE OF RECOMBINANT BOVINE INTERFERON-GAMMA AT 3.0 ANGSTROMS RESOLUTION

Overview

The three-dimensional crystal structure of recombinant bovine interferon-gamma was determined using the multiple isomorphous replacement method at 3.0 A and refined to an R factor of 19.2%. This protein crystallizes in space group P2(1)2(1)2(1) with unit-cell parameters of a = 42.8, b = 79.9 and c = 85.4 A. There is one functional dimer in the asymmetric unit. The two polypeptide chains are related by a non-crystallographic twofold symmetry axis. The secondary structure is predominantly alpha-helical with extensive interdigitation of the alpha-helical segments of the polypeptide chains that make up the dimer. The secondary structure, tertiary structure and topology of this molecule are identical to the previously reported structures of recombinant rabbit interferon-gamma and recombinant human interferon-gamma. The molecular topology is also similar to that of murine interferon-beta. These structural similarities strongly indicate the presence of a unique topological feature (fold) among gamma-interferons from different species, and also among the different classes of interferons.

About this Structure

1RFB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structure of recombinant bovine interferon-gamma at 3.0 A resolution., Samudzi CT, Rubin JR, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):513-21. PMID:15299487

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