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Figure 6 | BMC Structural Biology

Figure 6

From: Solution structure of the Legionella pneumophila Mip-rapamycin complex

Figure 6

Multiple sequence alignment of FKBPs and FKBDs from different organisms. The standard colouring pattern of ClustalX [57] is used. Well and strictly conserved residues that are associated with binding of rapamycin in human FKBP12 and in Mip77–213 are labelled by black boxes. The functional equivalents F-153 in Mip77–213 and F-46 in human FKBP12 (black circles) are neither conserved nor aligned to the same sequence position. Graphical representation of the rate of conservation is indicated at the bottom. Proteins shown: Legionella pneumophila Mip, <Q5ZXE0>; Homo sapiens FKBP12, <P62942>; Bos Taurus FKBP1A, <P18203>; baker's yeasts FPR1, <P20081>; Corynebacterium glutamicum Cgl0830, <P42458>; Escherichia coli FKPA, <P45523>; Trypanosoma cruzi Mip, <Q09734>.

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