1D0N
THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.
Summary for 1D0N
| Entry DOI | 10.2210/pdb1d0n/pdb |
| Descriptor | HORSE PLASMA GELSOLIN (2 entities in total) |
| Functional Keywords | mixed alpha-beta structure, actin-binding protein, protein domain packing, contractile protein |
| Biological source | Equus caballus (horse) |
| Total number of polymer chains | 2 |
| Total formula weight | 161383.09 |
| Authors | Burtnick, L.D.,Robinson, R.,Li, C. (deposition date: 1999-09-13, release date: 1999-09-15, Last modification date: 2024-10-30) |
| Primary citation | Burtnick, L.D.,Koepf, E.K.,Grimes, J.,Jones, E.Y.,Stuart, D.I.,McLaughlin, P.J.,Robinson, R.C. The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell(Cambridge,Mass.), 90:661-670, 1997 Cited by PubMed Abstract: The structure of gelsolin has been determined by crystallography and comprises six structurally related domains that, in a Ca2+-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. We propose that binding Ca2+ can release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. Domain shifts are proposed in response to Ca2+ as bases for models of how gelsolin acts to sever, cap, or nucleate F-actin filaments. The structure also invites discussion of polyphosphoinositide binding to segment 2 and suggests how mutation at Asp-187 could initiate a series of events that lead to deposition of amyloid plaques, as observed in victims of familial amyloidosis (Finnish type). PubMed: 9288746DOI: 10.1016/S0092-8674(00)80527-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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