%0 Figure %A Higo, Kunitake %A Ikura, Teikichi %A Oda, Masayuki %A Morii, Hisayuki %A Takahashi, Jun %A Abe, Ryo %A Ito, Nobutoshi %D 2013 %T Comparison of the structures of phosphopeptides bound to Grb2 SH2. %U https://plos.figshare.com/articles/figure/_Comparison_of_the_structures_of_phosphopeptides_bound_to_Grb2_SH2_/811084 %R 10.1371/journal.pone.0074482.g002 %2 https://plos.figshare.com/ndownloader/files/1219752 %K structures %K phosphopeptides %K bound %K grb2 %X

(A) CD28 (present work, D-pY-M-N-M-T). (B) BCR-Abl (a typical type-I β-turn, PDB ID: 1BMB, F-pY-V-N-V-E) (C) AICD (with a Pro residue at the pY+3 position, PDB ID: 3MXC, G-pY-E-N-P-T-Y). The SH2 domains are shown as surface models, whereas the phosphopeptides are shown as stick models. The thin green lines indicate the distance between the main-chain O of pY and the main-chain N of pY+3, which form a hydrogen bond in the type-I β-turn. The side-chains of some flanking residues are missing due to their weak electron density. (D) Superposition of the 3 peptides. The tubes represent the main-chain traces of CD28 (green), BCR-Abl (red), and AICD (blue). (E) Superposition of CD28, BCR-Abl, and AICD as in (D) but vertically rotated by approximately 90°.

%I PLOS ONE