Biochemical Properties | The two enzymes share >55% sequence identity, a similar 3D structure, and a common regulatory mechanism. However, they often perform opposite cellular functions, with SHP-1 typically acting as a negative regulator of signaling, whereas SHP-2 is a positive regulator. Some of the functional differences may be attributed to the SH2 domains, which display overlapping but non-identical binding specificities and may therefore direct their respective PTP domains to different pY proteins. |
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Bibliography | 1.Ren L, Chen X, Luechapanichkul R, Selner NG, Meyer TM, Wavreille AS, Chan R, Iorio C, Zhou X, Neel BG, Pei D. Substrate specificity of protein tyrosine phosphatases 1B, RPTPα, SHP-1, and SHP-2. Biochemistry. 2011 Mar 29;50(12):2339-56. doi: 10.1021/bi1014453. Epub 2011 Feb 18. PMID: 21291263; PMCID: PMC3074353. 2.Crystal structure of the tyrosine phosphatase SHP-2.Hof P, Pluskey S, Dhe-Paganon S, Eck MJ, Shoelson SE.Cell. 1998 Feb 20; 92(4):441-50. 3.Crystal structure of human protein-tyrosine phosphatase SHP-1.Yang J, Liu L, He D, Song X, Liang X, Zhao ZJ, Zhou GW.J Biol Chem. 2003 Feb 21; 278(8):6516-20. 4.Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains.Sweeney MC, Wavreille AS, Park J, Butchar JP, Tridandapani S, Pei D.Biochemistry. 2005 Nov 15; 44(45):14932-47. |