Supplementary Materials

An Exon Splice Enhancer Primes IGF2:IGF2R Binding Site Structure and Function Evolution

Christopher Williams, Hans-J├╝rgen Hoppe, Dellel Rezgui, Madeleine Strickland, Briony E. Forbes, Frank Grutzner, Susana Frago, Rosamund Z. Ellis, Pakorn Wattana-Amorn, Stuart N. Prince, Oliver J. Zaccheo, Catherine M. Nolan, Andrew J. Mungall, E. Yvonne Jones, Matthew P. Crump, A. Bassim Hassan

Materials/Methods, Supplementary Text, Tables, Figures, and/or References

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  • Materials and Methods
  • Supplementary Text
  • Figs. S1 to S14
  • Tables S1 to S4
  • References

Images, Video, and Other Other Media

Movie S1
The conformational dynamics induced in IGF2R domain 11 upon binding IGF2. The movie initially shows the solution structure of domain 11E4 in complex with IGF2 to illustrate the predominantly hydrophobic binding interface formed by the AB, CD, FG and HI loops. Colour coding is light blue: AB loop, wheat, CD, pale green, FG and light pink, HI. The surface of domain 11 is shown and IGF2 is rendered in red ribbons. The movie then goes on to show the changes in the binding site loops that occur upon binding IGF2. In particular, the conformation of the AB and FG loops can be seen to change significantly upon complex formation as they move to accommodate IGF2. These conformational changes help form a complimentary hydrophobic surface and modulate the interaction through the formation of new hydrogen bonds and salt bridges. The movie frames were generated using PyMOL 1.3 and encoded using Mencoder r32510-4.1.2. The Yale morph server was used to morph the unbound IGF2R-domain11E4 structure to the bound form (68).