7XC0
Crystal structure of Human RPTPH
Summary for 7XC0
| Entry DOI | 10.2210/pdb7xc0/pdb |
| Descriptor | Receptor-type tyrosine-protein phosphatase H, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | phosphatase, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 33322.48 |
| Authors | |
| Primary citation | Kim, M.,Ryu, S.E. Crystal structure of the catalytic domain of human RPTPH. Acta Crystallogr.,Sect.F, 78:265-269, 2022 Cited by PubMed Abstract: Receptor-type protein tyrosine phosphatases (RPTPs) receive extracellular stimuli and transfer them into cells. They regulate cell growth, differentiation and death via specific signals. They have also been implicated in cancer, diabetes and neurological diseases. RPTPH, a member of the type 3 RPTP (R3-PTP) family, is an important regulator of colorectal cancer and hepatic carcinoma. Despite its importance in drug development, the structure of RPTPH has not yet been resolved. Here, the crystal structure of the catalytic domain of RPTPH was determined at 1.56 Å resolution. Despite similarities to other R3-PTPs in its overall structure, RPTPH exhibited differences in its loop regions and side-chain conformations. Compared with other R3-PTPs, RPTPH has unique side chains near its active site that may confer specificity for inhibitor binding. Therefore, detailed information on the structure of RPTPH provides clues for the development of specific inhibitors. PubMed: 35787553DOI: 10.1107/S2053230X22006173 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
Download full validation report
