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Figure 1 | BMC Structural Biology

Figure 1

From: Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft

Figure 1

SHP-2 N-SH2 crystal structures. A) Crystal structure of isolated N-SH2 [PDB:1AYD] [9] showing the open pY-peptide binding cleft formed by the EF (red) and BG loops. B) Crystal structures of isolated N-SH2 [PDB:1AYD] (red), and N-SH2 in the full SHP-2 protein [PDB:2SHP] [4] (yellow). Dashed lines connect the Cα atoms of Gly67 and Asn92. Also shown are pY-peptides from N-SH2 – pY-peptide complexes [blue from PDB:1AYA and green from PDB:1AYB] [9]. All structures were RMS aligned to the Cα atoms of residues 6 to 55 of the SHP-2 crystal structure, which are structurally similar among the crystal structures. Molecular graphics were generated with VMD [45].

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