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 2.2Å" /> '''MACROPHAGE MIGRATION ...)
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Revision as of 12:49, 20 November 2007
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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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