Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation
AbstractCa2+ of 0.3–1.0 μM induces both the exposure of tryptic cleavage sites within the gelsolin m...
Khaitlina S, Hinssen H. Ca-dependent binding of actin to gelsolin. FEBS LETTERS. 2002;521(1-3):14-18...
We have purified the two functionally distinct domains of gelsolin, a Ca(2+)-dependent actin binding...
Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we p...
AbstractGelsolin requires activation to carry out its severing and capping activities on F-actin. He...
Rearrangement of the actin cytoskeleton occurs in a variety of cellular processes and structures and...
Khaitlina S, Walloscheck M, Hinssen H. Calcium-induced conformational changes in the C-terminal half...
Gelsolin belongs to a family of proteins that participates in the reorganization of cytoskeletal ac...
AbstractGelsolin is an actin-binding protein that is regulated by the occupancy of multiple calcium-...
The actin cytoskeleton is a complex structure that performs a wide range of cellular functions inclu...
AbstractThe structure of gelsolin has been determined by crystallography and comprises six structura...
The structure of gelsolin has been determined by crystallography and comprises six structurally rela...
Gelsolin, a multifunctional actin-modulating protein, has two actin-binding sites which may interact...
Hellweg T, Hinssen H, Eimer W. The Ca(2+)-induced conformational change of gelsolin is located in th...
Hellweg T, Hinssen H, Eimer W. The Ca(2+)-induced conformational change of gelsolin is located in th...
AbstractCa2+ of 0.3–1.0 μM induces both the exposure of tryptic cleavage sites within the gelsolin m...
Khaitlina S, Hinssen H. Ca-dependent binding of actin to gelsolin. FEBS LETTERS. 2002;521(1-3):14-18...
We have purified the two functionally distinct domains of gelsolin, a Ca(2+)-dependent actin binding...
Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we p...
AbstractGelsolin requires activation to carry out its severing and capping activities on F-actin. He...
Rearrangement of the actin cytoskeleton occurs in a variety of cellular processes and structures and...
Khaitlina S, Walloscheck M, Hinssen H. Calcium-induced conformational changes in the C-terminal half...
Gelsolin belongs to a family of proteins that participates in the reorganization of cytoskeletal ac...
AbstractGelsolin is an actin-binding protein that is regulated by the occupancy of multiple calcium-...
The actin cytoskeleton is a complex structure that performs a wide range of cellular functions inclu...
AbstractThe structure of gelsolin has been determined by crystallography and comprises six structura...
The structure of gelsolin has been determined by crystallography and comprises six structurally rela...
Gelsolin, a multifunctional actin-modulating protein, has two actin-binding sites which may interact...
Hellweg T, Hinssen H, Eimer W. The Ca(2+)-induced conformational change of gelsolin is located in th...
Hellweg T, Hinssen H, Eimer W. The Ca(2+)-induced conformational change of gelsolin is located in th...
AbstractCa2+ of 0.3–1.0 μM induces both the exposure of tryptic cleavage sites within the gelsolin m...
Khaitlina S, Hinssen H. Ca-dependent binding of actin to gelsolin. FEBS LETTERS. 2002;521(1-3):14-18...
We have purified the two functionally distinct domains of gelsolin, a Ca(2+)-dependent actin binding...