|Title||The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation|
|Publication Type||Journal Article|
|Year of Publication||1997|
|Authors||Burtnick, LD, Koepf, EK, Grimes, J, Jones, EY, Stuart, DI, McLaughlin, PJ, Robinson, RC|
|Type of Article||Article|
|Keywords||AMYLOIDOSIS, BINDING DOMAIN, calcium, DEFINITION, F-ACTIN, FILAMENT, IDENTIFICATION, PROTEIN, SEQUENCE, VILLIN|
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).
|URL||<Go to ISI>://A1997XT06600010|