Skip to main content


Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Figure 7 | BMC Structural Biology

Figure 7

From: Structural insights into Noonan/LEOPARD syndrome-related mutants of protein-tyrosine phosphatase SHP2 (PTPN11)

Figure 7

Q506 is necessary to position and activate a water molecule for hydrolysis of the phospho-enzyme intermediate (wild type). The Q506P mutant loses this functionality. Q506 also forms two important hydrogen bonds with Asn58 and Ala72 from the N-SH2 domain (colored in blue), which connect the N-SH2 domain to the PTP domain (colored in green). In the Q506P structure, these connections no longer are present. The P-loop (458–464) is highlighted in magenta.

Back to article page