1fim

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(New page: 200px<br /><applet load="1fim" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fim, resolution 2.2&Aring;" /> '''MACROPHAGE MIGRATION ...)
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[[Image:1fim.gif|left|200px]]<br /><applet load="1fim" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fim.gif|left|200px]]<br /><applet load="1fim" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fim, resolution 2.2&Aring;" />
caption="1fim, resolution 2.2&Aring;" />
'''MACROPHAGE MIGRATION INHIBITORY FACTOR'''<br />
'''MACROPHAGE MIGRATION INHIBITORY FACTOR'''<br />
==Overview==
==Overview==
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The tertiary structure of the macrophage migration inhibitory factor (MIF), from rat liver (12,300 Mr) is presented at 2.2 A resolution. Each monomer, consists of two beta/alpha/beta motifs aligned in quasi two-fold symmetry, comprising a domain consisting of a four-stranded mixed beta-sheet and two, antiparallel alpha-helices. The protein exists as a trimer in the crystal., An extra beta-strand that is almost perpendicular to the other, beta-strands joins to the beta-sheet of the neighbouring monomer in the, trimer. Unexpected similarities were detected between MIF and two kinds of, isomerase.
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The tertiary structure of the macrophage migration inhibitory factor (MIF) from rat liver (12,300 Mr) is presented at 2.2 A resolution. Each monomer consists of two beta/alpha/beta motifs aligned in quasi two-fold symmetry, comprising a domain consisting of a four-stranded mixed beta-sheet and two antiparallel alpha-helices. The protein exists as a trimer in the crystal. An extra beta-strand that is almost perpendicular to the other beta-strands joins to the beta-sheet of the neighbouring monomer in the trimer. Unexpected similarities were detected between MIF and two kinds of isomerase.
==About this Structure==
==About this Structure==
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1FIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FIM OCA].
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1FIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FIM OCA].
==Reference==
==Reference==
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[[Category: macrophage]]
[[Category: macrophage]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:57:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:04 2008''

Revision as of 10:39, 21 February 2008


1fim, resolution 2.2Å

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MACROPHAGE MIGRATION INHIBITORY FACTOR

Overview

The tertiary structure of the macrophage migration inhibitory factor (MIF) from rat liver (12,300 Mr) is presented at 2.2 A resolution. Each monomer consists of two beta/alpha/beta motifs aligned in quasi two-fold symmetry, comprising a domain consisting of a four-stranded mixed beta-sheet and two antiparallel alpha-helices. The protein exists as a trimer in the crystal. An extra beta-strand that is almost perpendicular to the other beta-strands joins to the beta-sheet of the neighbouring monomer in the trimer. Unexpected similarities were detected between MIF and two kinds of isomerase.

About this Structure

1FIM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the macrophage migration inhibitory factor from rat liver., Suzuki M, Sugimoto H, Nakagawa A, Tanaka I, Nishihira J, Sakai M, Nat Struct Biol. 1996 Mar;3(3):259-66. PMID:8605628

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