8Y8Y
Crystal structure of the PTPN21 FERM domain
Summary for 8Y8Y
| Entry DOI | 10.2210/pdb8y8y/pdb |
| Descriptor | Tyrosine-protein phosphatase non-receptor type 21, CHLORIDE ION (3 entities in total) |
| Functional Keywords | ptpn21, ferm, ptpd1, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34293.25 |
| Authors | |
| Primary citation | Lee, H.S.,Ku, B.,Shin, H.C.,Kim, S.J. Structural analysis of the FERM domain of human protein tyrosine phosphatase non-receptor type 21. Acta Crystallogr.,Sect.F, 80:148-153, 2024 Cited by PubMed Abstract: Protein tyrosine phosphatase non-receptor type 21 (PTPN21) is a cytosolic protein tyrosine phosphatase that regulates cell growth and invasion. Due to its oncogenic properties, PTPN21 has recently emerged as a potential therapeutic target for cancer. In this study, the three-dimensional structure of the PTPN21 FERM domain was determined at 2.1 Å resolution by X-ray crystallography. The crystal structure showed that this domain harbors canonical FERM folding and consists of three subdomains that are tightly packed via highly conserved intramolecular hydrophobic interactions. Consistent with this, the PTPN21 FERM domain shares high structural homology with several other FERM domains. Moreover, structural superimposition demonstrated two putative protein-binding sites of the PTPN21 FERM domain, which are presumed to be associated with interaction with its binding partner, kinesin family member 1C. Thus, these data suggest that the FERM domain of PTPN21 serves as a module that mediates protein-protein interaction, like other FERM domains. PubMed: 38940939DOI: 10.1107/S2053230X24005260 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.099 Å) |
Structure validation
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