1ZV6
NMR structure of the human dematin headpiece S74E mutant
Summary for 1ZV6
| Entry DOI | 10.2210/pdb1zv6/pdb |
| Related | 1QQV 1QZP 1VII |
| NMR Information | BMRB: 6718 |
| Descriptor | EPB49 protein (1 entity in total) |
| Functional Keywords | dematin headpiece, actin binding domain, phosphorylation, protein binding |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 7978.36 |
| Authors | Jiang, Z.G.,McKnight, C.J. (deposition date: 2005-06-01, release date: 2006-03-21, Last modification date: 2024-05-22) |
| Primary citation | Jiang, Z.G.,McKnight, C.J. A phosphorylation-induced conformation change in dematin headpiece. Structure, 14:379-387, 2006 Cited by PubMed Abstract: Dematin is an actin binding protein from the junctional complex of the erythrocyte cytoskeleton. The protein has two actin binding sites and bundles actin filaments in vitro. This actin bundling activity is reversibly regulated by phosphorylation in the carboxyl terminal "headpiece" domain (DHP). DHP is a typical villin-type headpiece actin binding motif and contains a flexible N-terminal loop and an alpha-helical C-terminal subdomain that is phosphorylated at Ser74. The NMR structure of a Ser74-to-Glu mutant (DHPs74e) closely mimics the conformation of phosphorylated DHP. The negative charge at Ser74 does not alter the conformation of the C-terminal subdomain, but attracts the N-terminal loop toward the C terminus, changing the orientation of the N-terminal subdomain. NMR relaxation studies also indicate reduced mobility in the N-terminal loop in DHPs74e. Thus, phosphorylation in DHP serves as a switch controlling the conformational state of DHP and the actin bundling activity of dematin. PubMed: 16472756DOI: 10.1016/j.str.2005.11.007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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