1ISN
Crystal structure of merlin FERM domain
Summary for 1ISN
| Entry DOI | 10.2210/pdb1isn/pdb |
| Descriptor | merlin (1 entity in total) |
| Functional Keywords | ferm domain, cell adhesion |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P46662 |
| Total number of polymer chains | 1 |
| Total formula weight | 38367.32 |
| Authors | Shimizu, T.,Seto, A.,Maita, N.,Hamada, K.,Tsukita, S.,Tsukita, S.,Hakoshima, T. (deposition date: 2001-12-13, release date: 2002-04-03, Last modification date: 2023-10-25) |
| Primary citation | Shimizu, T.,Seto, A.,Maita, N.,Hamada, K.,Tsukita, S.,Tsukita, S.,Hakoshima, T. Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain. J.Biol.Chem., 277:10332-10336, 2002 Cited by PubMed Abstract: Neurofibromatosis type 2 (NF2) is a dominantly inherited disease associated with the central nervous system. The NF2 gene product merlin is a tumor suppressor, and its mutation or inactivation causes this disease. We report here the crystal structure of the merlin FERM domain containing a 22-residue alpha-helical segment. The structure reveals that the merlin FERM domain consists of three subdomains displaying notable features of the electrostatic surface potentials, although the overall surface potentials similar to those of ezrin/radixin/moesin (ERM) proteins indicate electrostatic membrane association. The structure also is consistent with inactivation mechanisms caused by the pathogenic mutations associated with NF2. PubMed: 11756419DOI: 10.1074/jbc.M109979200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
