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Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
Published on: March 19, 2014
Top surface blade residues and the central channel water molecules are conserved in every repeat of the integrin-like
Alexander Denesyuk1, Konstantin Denessiouk2, Mark S Johnson3
1Faculty of Science and Engineering, Åbo Akademi University, Turku 20520, Finland; Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino 142290, Russia.
Abstract:
An integrin-like β-propeller domain contains seven repeats of a four-stranded antiparallel β-sheet motif (blades). Previously we described a 3D structural motif within each blade of the integrin-type β-propeller. Here, we show unique structural links that join different blades of the β-propeller structure, which together with the structural motif for a single blade are repeated in a β-propeller to provide the functional top face of the barrel, found to be involved in protein-protein interactions and substrate recognition. We compare functional top face diagrams of the integrin-type β-propeller domain and two non-integrin type β-propeller domains of virginiamycin B lyase and WD Repeat-Containing Protein 5.
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