1fim
MACROPHAGE MIGRATION INHIBITORY FACTORMACROPHAGE MIGRATION INHIBITORY FACTOR
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|